P4HB / ERBA2L recombinant protein

Recombinant Mouse P4HB / ERBA2L Protein (His tag)

Cat. Num. AAA2546875

• Gene Names: P4hb; PDI; Thbp; ERp59; Pdia1
• Purity: > 95 % as determined by SDS-PAGE
• Synonyms: P4HB / ERBA2L; Recombinant Mouse P4HB / ERBA2L Protein (His tag); RP23-84C12.2; ERp59; PDI; Pdia1; Thbp; P4HB / ERBA2L recombinant protein

• Host: Human Cells
• Purity/Purification: > 95 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH 7.4
• Sequence Length: 509

• Application Notes: The secreted recombinant mouse P4HB comprises 498 amino acids and has a calculated molecular mass of 56.2 kDa as estimated in SDS-PAGE under reducing conditions.
• Predicted N Terminal: Asp 20
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

Related Product Information for P4HB / ERBA2L recombinant protein

Background: Mouse protein disulfide-isomerase, also known as Cellular thyroid hormone-binding protein, Prolyl 4-hydroxylase subunit beta, p55 and P4HB, is a peripheral membrane protein which belongs to the protein disulfide isomerase family. P4HB is highly abundant. In some cell type s, it seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. P4HB localizes near CD4-enriched regions on lymphoid cell surfaces. It is identified by mass spectrometry in melanosome fractions from stage I to stage IV. P4HB reduces and may activate fusogenic properties of HIV-1 gp120 surface protein, thereby enabling HIV-1 entry into the cell. P4HB catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, it seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. P4HB may therefore cause structural modifications of exofacial proteins. Inside the cell, it seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, P4HB functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, it facilitates aggregation (anti-chaperone activity). P4HB may be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. It also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.

Description: A DNA sequence encoding the mouse P4HB (NP_035162.1) (Met 1-Lys 506) was expressed, with a C-terminal polyhistidine tag.

NCBI and Uniprot Product Information

• NCBI GI #: 42415475
• NCBI GeneID: 18453
• NCBI Accession #: NP_035162.1
• NCBI GenBank Nucleotide #: NM_011032.2
• UniProt Accession #: P09103; Q922C8
• Molecular Weight: 57,058 Da
• NCBI Official Full Name: protein disulfide-isomerase
• NCBI Official Synonym Full Names: prolyl 4-hydroxylase, beta polypeptide
• NCBI Official Symbol: P4hb
• NCBI Official Synonym Symbols: PDI; Thbp; ERp59; Pdia1
• NCBI Protein Information: protein disulfide-isomerase
• UniProt Protein Name: Protein disulfide-isomerase
• UniProt Gene Name: P4hb
• UniProt Synonym Gene Names: Pdia1; PDI; ER protein 59; ERp59

Uniprot Description

PDIA1: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity. Binds UBQLN1. Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex. Belongs to the protein disulfide isomerase family.

Protein type: EC 5.3.4.1; Endoplasmic reticulum; Isomerase; Nuclear receptor co-regulator; Oxidoreductase

Chromosomal Location of Human Ortholog: 11 E2|11 84.27 cM

Cellular Component: endoplasmic reticulum; ER-Golgi intermediate compartment; external side of plasma membrane; extracellular matrix; focal adhesion

Molecular Function: enzyme binding; integrin binding; peptidyl-proline 4-dioxygenase activity; procollagen-proline 4-dioxygenase activity; protein binding; protein disulfide isomerase activity; protein heterodimerization activity

Biological Process: peptidyl-proline hydroxylation to 4-hydroxy-L-proline; positive regulation of virion penetration into host cell; protein folding