protein

Recombinant Protein Disulfide Isomerase (PDI)

MBS2010145

0.01 mg

185 USD

Recombinant Protein

Recombinant Protein Disulfide Isomerase (PDI)

Protein Disulfide Isomerase (PDI)

protein disulfide-isomerase; Protein disulfide-isomerase; protein disulfide-isomerase; p55; ER protein 59; protein disulfide isomerase; prolyl 4-hydroxylase subunit beta; cellular thyroid hormone-binding protein; endoplasmic reticulum resident protein 59; prolyl 4-hydroxylase, beta polypeptide; Cellular thyroid hormone-binding protein; Endoplasmic reticulum resident protein 59; ER protein 59; ERp59; Prolyl 4-hydroxylase subunit beta; p55

PDI

P4hb; P4hb; PDI; Thbp; ERp59; Pdia1; Pdia1; PDI; ER protein 59; ERp59

PDIA1_MOUSE

E Coli

509

The target protein is fused with two N-terminal Tags, His-tag and GST-tag, its sequence is listed below. MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD GSTSGSGHHH HHHSAGLVPR GSTAIGMKET AAAKFERQHM DSPDLGTLEV LFQGPLGS-DEGRNNFEG EITKEKLLDF IKHNQLPLVI EFTEQTAPKI FGGEIKTHIL LFLPKSVSDY DGKLSSFKRA AEGFKGKILF IFIDSDHTDN QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITEFCHRFLE GKIKPHLMSQ EVPEDWDKQP VKVLVGANFE EVAFDEKKNV FVEFYAPWCG HCKQLAPIWD KLGETYKDHE NIIIAKMDST ANEVEAVKVH SFPTLKFFPA SADRTVIDYN GER

> 95%

Supplied as lyophilized form in 20mM Tris, 150mM NaCl, pH8.0, containing 1mM EDTA, 1mM DTT, 0.01% sarcosyl, 5% trehalose, and preservative.

Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months. Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test,that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. (Referring from China Biological Products Standard,which was calculated by the Arrhenius equation.) The loss of this protein is lessthan 5% within the expiration date under appropriate storage condition.

SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)

Organism: Mus musculus (Mouse). Expression System: Prokaryotic expression. Residues: Asp212~Arg463 (Accession # P09103) with two N-terminal Tags, His-tag and GST-tag. Subcellular Location: Endoplasmic reticulum lumen. Melanosome. Cell membrane; Peripheral membrane protein

Endotoxin Level: <1.0EU per 1ug (determined by the LAL method). Predicted Isoelectric Point: 5.7. Reconstitution: Reconstitute in sterile PBS, pH7.2-pH7.4.

About the Marker: Effective Size Range: 10kDa to 70kDa. Protein bands: 10kDa, 14kDa, 18kDa, 22kDa, 26kDa, 33kDa, 44kDa and70kDa. Double intensity bands: The 26kDa, 18kDa, 10kDa bands are at doubleintensity to make location and size approximation of proteins of interestquick and easy. Ready-to-use: No need to heat, dilute or add reducing agents before use.

42415475

NP_035162.1

NM_011032.2

P09103

60.8kDa

Cellular Responses To Stress Pathway (925999); Chylomicron-mediated Lipid Transport Pathway (926692); Collagen Biosynthesis And Modifying Enzymes Pathway (927063); Collagen Formation Pathway (927062); Detoxification Of Reactive Oxygen Species Pathway (926005); Extracellular Matrix Organization Pathway (927061); Lipid Digestion, Mobilization, And Transport Pathway (926688); Lipoprotein Metabolism Pathway (926691); Metabolism Pathway (926669); Metabolism Of Lipids And Lipoproteins Pathway (926687)

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: Isomerase; Nuclear receptor co-regulator; EC 5.3.4.1; Endoplasmic reticulum; Oxidoreductase. Cellular Component: focal adhesion; membrane; endoplasmic reticulum; plasma membrane; ER-Golgi intermediate compartment. Molecular Function: enzyme binding; procollagen-proline 4-dioxygenase activity; protein heterodimerization activity; protein disulfide isomerase activity; isomerase activity; peptidyl-proline 4-dioxygenase activity. Biological Process: protein folding; cell redox homeostasis; peptidyl-proline hydroxylation to 4-hydroxy-L-proline

0.01 mg

185 USD

0.05 mg

385

0.1 mg

595