Immunohistochemistry-Paraffin: Bag-1 Antibody [NB100-56081] - Formalin-fixed, paraffin-embedded sections of human colorectal cancer stained for Bag-1 using this antibody at 1:2000. Hematoxylin-eosin counterstain. ...read more
Immunohistochemistry-Paraffin: Bag-1 Antibody [NB100-56081] - Formalin-fixed, paraffin-embedded section of human colon stained for Bag-1 using this antibody at 1:2000. Hematoxylin-eosin counterstain.
Novus Biologicals Rabbit Bag-1 Antibody - BSA Free (NB100-56081) is a polyclonal antibody validated for use in IHC, WB and IP. Anti-Bag-1 Antibody: Cited in 1 publication. All Novus Biologicals antibodies are covered by our 100% guarantee.
Immunogen
A synthetic peptide corresponding to amino acids 205-219 (QETERLQSTNLALAE) of mouse BAG-1 was used as immunogen; GenBank no. AAH03722.1. This sequence is 100% conserved in mouse BAG-1L; GenBank no. NP_033866.3.
Isotype
IgG
Clonality
Polyclonal
Host
Rabbit
Gene
BAG1
Purity
Unpurified
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Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
Buffer
Whole antisera
Preservative
0.02% Sodium Azide
Purity
Unpurified
Alternate Names for Bag-1 Antibody - BSA Free
BAG family molecular chaperone regulator 1
Bag1
Bag-1
Bcl-2 associating athanogene-1 protein
Bcl-2-associated athanogene 1
BCL2-associated athanogene
Bcl-2-binding protein
glucocortoid receptor-associated protein RAP46,46-KD
HAP
RAP46
Background
The BAG (Bcl-2-associated anthanogene) proteins are a family of chaperone regulators that modulate several diverse processes including proliferation, survival, stress responses, tumorigenesis, neuronal differentiation, growth arrest and apoptosis (reviewed Takayama and Reed, 2001; Doong et al, 2002, and Doukhanina et al. 2006). BAG proteins have been characterized as co-chaperones and interact with the chaperone heat shock proteins 70, both constitutive Hsc70 and inducible Hsp70. BAG proteins bind through their BAG domain to the ATPase domain of Hsc70/Hsp70 and can modulate either positively or negatively the functions of the Hsc70/Hsp70 chaperone proteins. The BAG domain has been shown to contribute to the anti-apoptotic activity of BAG- family proteins. The anti-apoptotic activities of BAG-family proteins may be dependent on their interactions with Hsc70/Asp70 and/or binding to Bcl-2. In addition to the conserved BAG domain, BAG-family proteins also contain additional domains which enable them to interact with specific target proteins or to target them to specific locations within cells. The BAG family contains at least six family members, including BAG-1 and its various isoforms [including BAG-1S, BAG-1M (Rap46/Hap46), and BAG-1L, BAG-2, BAG-3 (CAIR-1/Bis,), BAG-4 (SODD), BAG-5 and BAG-6 (Scythe, BAT3). The following amino acids lengths and molecular weights (kDa) have been described for human BAG proteins (reviewed in Takayama et al, 2001 and Doong et al, 2002): BAG-1 (230 amino acid., 34 kDa), BAG-1S (219 amino acid, 29 kDa), BAG-1M (274 amino acid, 46 kDa), BAG-1L (345 amino acid, 52 kDa), BAG-2 [212 amino acid; 24 kDa (Arndt et al. 2005)], BAG-3 (575 amino acid, 74 kDa), BAG-4 (456 amino acid; 60 kDa), BAG-5 ([442 amino acid; 51 kDa (Kalia et al. 2004)], and BAG-6 (1129 amino acid; 150 kDa). Recognizes both BAG-1 and BAG-1 isoforms which contain the peptide immunogen sequence, including BAG-1L. Mouse BAG-1 is a 219 amino acid protein (GenBank no. AAH03722.1) and mouse BAG-1L is a 355 amino acid protein (AAH03722.1).
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.
BAG3 - Hsp70 is my friend! The BAG proteins are a large family of chaperone regulators governing a wide range of cell processes such as proliferation, survival, stress response, tumorigenesis, neuronal differentiation, growth arrest and apoptosis as reviewed in Takayama et al1.... Read full blog post.
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