ASPH (75-270, His-tag) Human Protein

CAT#: AR09383PU-L

ASPH (75-270, His-tag) human recombinant protein, 0.5 mg

Product Images

Specifications

Product Data

• Species: Human
• Expression Host: E. coli
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT
• Tag: His-tag
• Predicted MW: 24.5 kDa
• Concentration: lot specific
• Purity: >90% by SDS - PAGE
• Buffer: Presentation State: Purified
  State: Liquid purified protein
  Buffer System: 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM DTT, 10% glycerol
• Preparation: Liquid purified protein
• Protein Description: Recombinant human ASPH protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
• Storage: Store undiluted at 2-8°C for up to two weeks or (in aliquots) at -20°C or -70°C for longer.
  Avoid repeated freezing and thawing.
• Stability: Shelf life: one year from despatch.

Reference Data

• RefSeq: NP_001158222
• Locus ID: 444
• UniProt ID: Q12797
• Cytogenetics: 8q12.3
• Synonyms: AAH; BAH; CASQ2BP1; FDLAB; HAAH; JCTN; junctin
• Summary: 'This gene is thought to play an important role in calcium homeostasis. The gene is expressed from two promoters and undergoes extensive alternative splicing. The encoded set of proteins share varying amounts of overlap near their N-termini but have substantial variations in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the epidermal growth factor (EGF)-like domains of some proteins, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Other isoforms differ primarily in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum. Some of these isoforms are found in complexes with calsequestrin, triadin, and the ryanodine receptor, and have been shown to regulate calcium release from the sarcoplasmic reticulum. Some isoforms have been implicated in metastasis. [provided by RefSeq, Sep 2009]'
• Protein Families: Druggable Genome, Transmembrane