CD38 Antibody (AT13/5) - Chimeric - Azide and BSA Free

Immunocytochemistry/Immunofluorescence: CD38 Antibody (AT13/5) [NBP2-81055] - Immunofluorescence staining of fixed Daudi cells with anti-CD38 antibody AT13/5 [NBP2-81055]. Immunofluorescence analysis of paraformaldehyde fixed Daudi cells on Shi-fix coverslips, permeabilized with 0.15% Triton and stained with the chimeric rabbit IgG version of AT13/5 [NBP2-81055] at 10 ug/mL for 1h followed by Alexa Fluor 488 secondary antibody (1 ug/mL), showing membrane staining. The nuclear stain is DAPI (blue). Panels show from left-right, top-bottom NBP2-81055, DAPI, merged channels and an isotype control. The isotype control was stained with an anti-Fluorescein antibody followed by Alexa Fluor 488 secondary antibody.

Western Blot: CD38 Antibody (AT13/5) [NBP2-81055] - Western Blot using anti-CD38 antibody (AT13/5) [NBP2-81055]. Human spleen lysate samples (35 ug protein in RIPA buffer) were resolved on a 10% SDS PAGE gel and blots probed with the chimeric rabbit version of AT13/5 [NBP2-81055] at 1 ug/mL before detection using an anti-rabbit secondary antibody. A primary incubation of 1h was used and protein was detected by chemiluminescence. The expected running size for CD38 is 34.3 kDa, but this protein is glycosylated at several residues. NBP2-81055 successfully detected CD38 in human spleen lysate.

• Reactivity: Hu
• Applications: WB, Flow, ICC/IF
• Clone: AT13/5
• Clonality: Monoclonal
• Host: Rabbit
• Conjugate: Unconjugated
• Format: Azide and BSA Free
• Concentration: 1 mg/ml

CD38 Antibody (AT13/5) - Chimeric - Azide and BSA Free Summary

• Description: This chimeric rabbit antibody was made using the variable domain sequences of the original Mouse IgG1 format, for improved compatibility with existing reagents, assays and techniques. The antibody binds to CD38, a glycoportein on the surface of various immune cells that catalyzes the hydrolysis of cyclic ADP-ribose to NAD+ and ADP-ribose.
• Additional Information: Recombinant Monoclonal Antibody. Clone AT13/5 was used by HLDA to establish CD designation.
• Immunogen: Namalwa cells emulsified in CFA
• Specificity: Binds specifically to human CD38, an approximately 45 kDa type II transmembrane protein, expressed on essentially all pre-B lymphocytes, plasma cells, and thymocytes. Also present on activated T lymphocytes, natural killer (NK) lymphocytes, myeloblasts, and erythroblasts. Bimodally expressed during B cell development, modulating from high in immature cells to low in intermediate ones and back to high on mature B cells. This antibody competes with clone HB7 (Ellis 1995) which has been shown to bind to an epitope between amino acids 273-285.
• Isotype: IgG Kappa
• Clonality: Monoclonal
• Host: Rabbit
• Gene: CD38
• Purity: Protein A purified

Applications/Dilutions

• Dilutions:
  • Flow Cytometry
  • Immunocytochemistry/ Immunofluorescence
  • Western Blot

Packaging, Storage & Formulations

• Storage: Store at 4C for up to 3 months. For longer storage, aliquot and store at -20C.
• Buffer: PBS
• Preservative: 0.02% Proclin 300
• Concentration: 1 mg/ml
• Purity: Protein A purified

Alternate Names for CD38 Antibody (AT13/5) - Chimeric - Azide and BSA Free

• 2'-phospho-ADP-ribosyl cyclase
• 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase (EC:2.4.99.20)
• 2'-phospho-cyclic-ADP-ribose transferase
• ADPRC 1
• ADPRC1
• ADP-ribosyl cyclase 1
• ADP-ribosyl Cyclase
• ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
• ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
• cADPr hydrolase 1
• CD_antigen: CD38
• CD38 antigen (p45)
• CD38 antigen
• CD38 molecule
• CD38
• cluster of differentiation 38
• Cyclic ADP-ribose hydrolase 1
• Cyclic ADP-ribose Hydrolase
• EC 2.4.99.20
• EC 3.2.2.6
• EC:3.2.2.6
• NAD(+) nucleosidase
• T10

Background

CD38 (cluster of differentiation 38), previously known as T10, is a 46 kDa type II transmembrane glycoprotein (1). CD38 is expressed in both lymphoid and non-lymphoid tissue including in thymocytes, T and B lymphocytes, myeloid cells, natural killer cells, plasma cells, erythrocytes, and additionally in cells of the brain, pancreas, muscle, and bone (1,2). Structurally, CD38 is an "L"-shape which is formed by two separate domains connected by a three peptide-chain hinge region (2). The N-terminal domain is composed of five alpha-helices and two beta strands, while the C-terminal domain contains a four-stranded parallel beta-sheet and two long and two short alpha-helices (2). The CD38 molecule is located on chromosome 4 and is 300 amino acids (aa) in length with a theoretical molecular weight of 34 kDa that functions as both a receptor and an enzyme (1-6). As a receptor, CD38 interacts with its ligand CD31, which is largely expressed in endothelial cells (2-6). As an ectoenzyme, CD38 has a role in calcium signaling and is responsible for the conversion of nicotinamide adenine dinucleotide (NAD) into adenosine diphosphate-ribose (ADPR) or cyclic ADPR and the conversion of phosphorylated NAD (NADP) into nicotinic acid adenine dinucleotide phosphate (NAADP) (2-6).

As described above, CD38 is highly expressed in plasma cells and, as a result, is a target for treating multiple myeloma (MM), the cancer of white blood cells (4,6). The anti-CD38 monoclonal antibody daratumumab is one specific treatment for MM (4,6). Daratumumab has been shown to target MM cells through antibody-dependent cellular cytotoxicity and antibody dependent cellular phagocytosis (4). Additionally, CD38 has a potential role in neurodegenerative disorders and neuroinflammation as elucidated CD38's high expression in neurons, astrocytes, and microglia along with its enzymatic role in NAD degradation (3). Reduced NAD levels is a consequence of aging and occurs during neurodegeneration (3). Furthermore, murine studies have found that CD38 deletion inhibits neuroinflammation and neurodegeneration and therefore might be a potential therapeutic target (3). Similarly, CD38 inhibitors, like quercetin and luteolin, are used to treat age-related diseases and metabolic disorders (7).

References

1. Malavasi, F., Funaro, A., Alessio, M., DeMonte, L. B., Ausiello, C. M., Dianzani, U., Lanza, F., Magrini, E., Momo, M., & Roggero, S. (1992). CD38: a multi-lineage cell activation molecule with a split personality. International journal of clinical & laboratory research. https://doi.org/10.1007/BF02591400

2. Malavasi, F., Deaglio, S., Funaro, A., Ferrero, E., Horenstein, A. L., Ortolan, E., Vaisitti, T., & Aydin, S. (2008). Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology. Physiological reviews. https://doi.org/10.1152/physrev.00035.2007

3. Guerreiro, S., Privat, A. L., Bressac, L., & Toulorge, D. (2020). CD38 in Neurodegeneration and Neuroinflammation. Cells. https://doi.org/10.3390/cells9020471

4. van de Donk, N., Richardson, P. G., & Malavasi, F. (2018). CD38 antibodies in multiple myeloma: back to the future. Blood. https://doi.org/10.1182/blood-2017-06-740944

5. Lund, F. E., Cockayne, D. A., Randall, T. D., Solvason, N., Schuber, F., & Howard, M. C. (1998). CD38: a new paradigm in lymphocyte activation and signal transduction. Immunological reviews. https://doi.org/10.1111/j.1600-065x.1998.tb01573.x

6. Glaria, E., & Valledor, A. F. (2020). Roles of CD38 in the Immune Response to Infection. Cells. https://doi.org/10.3390/cells9010228

7. Rajman, L., Chwalek, K., & Sinclair, D. A. (2018). Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence. Cell metabolism. https://doi.org/10.1016/j.cmet.2018.02.011

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

FAQs for CD38 Antibody (NBP2-81055). (Showing 1 - 1 of 1 FAQ).

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Bioinformatics

• Gene Symbol: CD38