Recombinant Mouse Chymase (Cma1), partial

Recombinant Mouse Chymase (Cma1), partial is a purified Recombinant Protein. Purity: >90% as determined by SDS-PAGE. Host: E. coli. Endotoxin Level: Not Tested. Species: Mouse (Mus musculus) . Target Name: Cma1. Target Synonyms: Alpha-chymase; Mast cell chymase 1Mast cell protease 5; mMCP-5Mast cell protease I. Accession Number: P21844. Expression Region: 22~246aa. Tag Info: N-Terminal 6Xhis-Tagged. Theoretical MW: 29.2kDa. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Storage: -20°C. Avoid repeated freeze/thaw cycles. Restrictions: For Research Use Only. Not for use in diagnostic procedures.

Product Specifications

CAS Number

9000-83-3

Short Description

Recombinant Mouse Chymase (Cma1), partial is a purified Recombinant Protein.

Accession Number

P21844

Expression Region

22~246aa

Host

E. coli

Target

Cma1

Conjugation

Unconjugated

Tag

N-Terminal 6Xhis-Tagged

Endotoxin

Not Tested

Purity

>90% by SDS-PAGE

Activity

Not Tested

Length

Partial

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Reconstitution

Refer to the datasheet/CoA included in the product pouch.

Molecular Weight

29.2kDa

Shipping Conditions

Ice packs

Storage Conditions

-20°C. Avoid repeated freeze/thaw cycles.

Target Alternative Name

Alpha-chymase; Mast cell chymase 1Mast cell protease 5; mMCP-5Mast cell protease I

Species

Mouse (Mus musculus)

Protein Name

Recombinant Protein

AA Sequence

IIGGTECIPHSRPYMAYLEIVTSENYLSACSGFLIRRNFVLTAAHCAGRSITVLLGAHNKTSKEDTWQKLEVEKQFLHPKYDENLVVHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPASDTLQEVKMRLQEPQACKHFTSFRHNSQLCVGNPKKMQNVYKGDSGGPLLCAGIAQGIASYVHRNAKPPAVFTRISHYRPWINKILRE