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SerpinA10 Protein, Mouse, Recombinant (His Tag)

Product Specifications

Background

Protein Z-dependent protease inhibitor, also known as PZ-dependent protease inhibitor, SERPINA1 and ZPI, is a secreted protein that belongs to the serpin family. It is expressed by the liver and secreted in plasma. SERPINA1 / Serpin-A1 inhibits factor Xa activity in the presence of protein Z, calcium and phospholipid. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors) . Over 1 serpins have now been identified, these include 36 human proteins, as well as molecules in plants, fungi, bacteria, archaea and certain viruses. Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin) . Most inhibitory serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic cysteine residue, rather than a serine residue, in their catalytic site.

Overview

A DNA sequence encoding the mature form of mouse SERPINA10 isoform 1 (Q8R121-1) (Met 1-Leu 448) was fused with a polyhistidine tag at the C-terminus.

Synonyms

PZI Protein, Mouse; Serpin A10 Protein, Mouse; ZPI Protein, Mouse

Gene Name

Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 10

UniProt

Q8R121-1

Expression System

HEK293 Cells

Tag

C-His

Endotoxin

< 1.0 EU per μg of the protein as determined by the LAL method.

Purity

> 95 % as determined by SDS-PAGE.

Activity

At Leading Biology, the biological activity of a recombinant protein is routinely measured using a bioassay, e.g. chemotaxis or cell proliferation assay, enzyme assay, or a functional ELISA. When a recombinant protein is an enzyme, specific activity is derived from an enzymatic assay. Each enzyme is tested for potency by cleavage of a substrate. We are in the process of updating the biological activity data. If you have any questions regarding this update, please feel free to contact our technical support team.

Form

Lyophilized

Buffer

Lyophilized from sterile PBS, pH 7.4. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.

Function

Enzyme Proteins

Molecular Weight

The secreted recombinant mouse SERPINA10 comprises 438 amino acids with a predicted molecular mass of 51 kDa. As a result of glycosylation, the apparent molecular mass of the protein is approximately 60-80 kDa in SDS-PAGE under reducing conditions.

Storage Conditions

In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.

Symbol

SerpinA10

Species

Mouse

Uniprot URL

https://www.uniprot.org/uniprot/Q8R121-1

AA Sequence

Met1-Leu448

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