Recombinant human PTP1B protein (Active) (ab51277)
Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Active: Yes
- Suitable for: SDS-PAGE, Functional Studies
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Product name
Recombinant human PTP1B protein (Active)
See all PTP1B proteins and peptides -
Biological activity
Specific activity is > 10,000 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C.
Activity Assay:- Prepare a 180ul assay buffer into a suitable container: The concentrations are 11mM Tris-HCl pH7.5, 55mM NaCl, 2.2mM DTT, 1.1mM MnCl2, 1.1mM EDTA, 33mM pNPP.
- Equilibrate to 37? and monitor the A405nm until value is constant using a spectrophotometer.
- Add 20ul of recombinant PTP-1B protein 12.5ug/ml in 0.1% BSA/DW.
- Record the absorbance A405nm for 5 minutes.
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Purity
> 95 % SDS-PAGE.
This protein was purified by conventional column chromatographic techniques. -
Expression system
Escherichia coli -
Accession
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Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
MEMEKEFEQI DKSGSWAAIY QDIRHEASDF PCRVAKLPKN KNRNRYRDVS PFDHSRIKLH QEDNDYINAS LIKMEEAQRS YILTQGPLPN TCGHFWEMVW EQKSRGVVML NRVMEKGSLK CAQYWPQKEE KEMIFEDTNL KLTLISEDIK SYYTVRQLEL ENLTTQETRE ILHFHYTTWP DFGVPESPAS FLNFLFKVRE SGSLSPEHGP VVVHCSAGIG RSGTFCLADT CLLLMDKRKD PSSVDIKKVL LEMRKFRMGL IQTADQLRFS YLAVIEGAKF IMGDSSVQDQ WKELSHEDLE PPPEHIPPPP RPPKRILEPH N -
Predicted molecular weight
37 kDa -
Amino acids
1 to 321 -
Additional sequence information
(NP_002818)
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Preparation and Storage
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Alternative names
- PTP1B
- Non receptor tyrosine phosphatase 1
- Protein phosphotyrosylphosphatase 1B
see all -
Function
May play an important role in CKII- and p60c-src-induced signal transduction cascades. -
Sequence similarities
Belongs to the protein-tyrosine phosphatase family. Non-receptor class 1 subfamily.
Contains 1 tyrosine-protein phosphatase domain. -
Post-translational
modificationsOxidized on Cys-215; the Cys-SOH formed in response to redox signaling reacts with the alpha-amido of the following residue to form a 4-amino-3-isothiazolidinone serine cross-link, triggering a conformational change that inhibits substrate binding and activity. The active site can be restored by reduction. -
Cellular localization
Endoplasmic reticulum membrane. - Information by UniProt