BPGM Recombinant Protein

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SDS-Page: BPGM Protein [NBP1-44485] - BPGM, 31kDa (267aa), confirmed by MALDI-TOF with a purity of 95% by SDS - PAGE

Product Details

Summary
Reactivity HuSpecies Glossary
Applications PAGE
Concentration
0.5 mg/ml

Order Details

BPGM Recombinant Protein Summary

Description
A recombinant protein with a His-tag corresponding to amino acids 1 to 259 of Human BPGM

Source: E. coli

Amino Acid Sequence: MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR EQMALNHGEE QVRLWRRSYN VTPPPIEESH PYYQEIYNDR RYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG KTILISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA IQAAIKKVED QGKVKQAKKL EHHHHHH
Preparation
Method
E.coli
Gene
BPGM
Purity
>95% pure by SDS-PAGE

Packaging, Storage & Formulations

Storage
Store at -80C. Avoid freeze-thaw cycles.
Conjugate
Unconjugated
Buffer
20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol
Preservative
No Preservative
Concentration
0.5 mg/ml
Purity
>95% pure by SDS-PAGE

Applications/Dilutions

Theoretical MW
31 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Reactivity Notes

This is a Human protein

Notes

The purity of this protein is > 95% by SDS-PAGE. Molecular weight is 31kDa (267aa), confirmed by MALDI-TOF

Alternate Names for BPGM Recombinant Protein

  • 2,3-bisphosphoglycerate mutase
  • bisphosphoglycerate mutase
  • BPG-dependent PGAM
  • EC 3.1.3.132,3-bisphosphoglycerate synthase
  • EC 5.4.2.1
  • EC 5.4.2.4
  • erythrocyte 2,3-bisphosphoglycerate mutase2,3-bisphosphoglycerate mutase, erythrocyte

Background

Bisphosphoglycerate mutase (BPGM) is an enzyme unique to erythrocytes and placental cells. This protein plays a major role in regulating hemoglobin oxygen affinity as a consequence of controlling 2,3-BPG concentration. It is responsible for the catalytic synthesis of 2,3-Bisphosphoglycerate (2,3-BPG) from 1,3-BPG. BPGM also has a mutase and a phosphatase function, but these are much less active. Recombinant human BPGM, fused to His-tag at C-terminus, was expressed in E.coli and purified by using conventional chromatography techniques

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

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Contact Information

Product PDFs

Bioinformatics

Gene Symbol BPGM

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