供货周期: | 现货 |
品牌: | 康朗生物 |
规格: | 50ug/100ug/250ug |
货号: | KL479Hu01 |
CAS号: |
肝素结合性表皮生长因子(HBEGF)重组蛋白
来源原核表达
宿主E.coli
内毒素水平<1.0EU/μg(LAL法测定)
亚细胞定位n/a
预测分子量17.2kDa
实际分子量-(差异分析请参阅说明书)
片段与标签Val21~Thr160 with N-terminal His Tag
缓冲液成份磷酸盐缓冲液(pH7.4,含有 0.01% SKL, 1mM DTT, 5% Trehalose和Proclin300.)
性状冻干粉
纯度> 95%
等电点-
肝素结合性表皮生长因子(HBEGF)重组蛋白应用SDS-PAGE; WB; ELISA; IP
Recombinant Matrix Gla Protein (MGP)
Organism Species: Homo sapiens (Human)
Instruction manual
FOR IN VITRO USE AND RESEARCH USE ONLY
NOT FOR USE IN CLINICAL DIAGNOSTIC PROCEDURES
10th Edition (Revised in Jan, 2014)
[ PROPERTIES ]
Residues: Met1~Lys103
Tags: Two N-terminal Tags, His-tag and T7-tag
Accession: P08493
Host: E. coli
Subcellular Location: Secreted.
Purity: >95%
Endotoxin Level: <1.0EU per 1μg
(determined by the LAL method).
Formulation: Supplied as lyophilized form in 20mM Tris,
150mM NaCl, pH8.0, containing 1mM EDTA, 1mM DTT,
0.01% sarcosyl, 5% trehalose, and preservative.
Predicted isoelectric point: 9.8
Predicted Molecular Mass: 16.2kDa
Applications: SDS-PAGE; WB; ELISA; IP.
(May be suitable for use in other assays to be determined by the end user.)
肝素结合性表皮生长因子(HBEGF)重组蛋白[ USAGE ]
Reconstitute in ddH2O.
[ STORAGE AND STABILITY ]
Storage: Avoid repeated freeze/thaw cycles.
Store at 2-8oC for one month.
Aliquot and store at -80oC for 12 months.
Stability Test: The thermal stability is described by the loss rate of the target
protein. The loss rate was determined by accelerated thermal degradation test,
that is, incubate the protein at 37oC for 48h, and no obvious degradation and
precipitation were observed. (Referring from China Biological Products Standard,
which was calculated by the Arrhenius equation.) The loss of this protein is less
than 5% within the expiration date under appropriate storage condition.
[ SEQUENCES ]
The sequence of the target protein is listed below.
MKSLILLAIL AALAVVTLCY ESHESMESYE LNPFINRRNA NTFISPQQRW RAKVQERIRE
RSKPVHELNR EACDDYRLCE RYAMVYGYNA AYNRYFRKRR GTK
肝素结合性表皮生长因子(HBEGF)重组蛋白[ REFERENCES ]
1. Cancela M.L., et al. (1990) J. Biol. Chem. 265:15040-15048. 2. Kiefer M.C., et al. (1988) Nucleic Acids Res. 16:5213-5213. 3. Chen L., et al. (1990) Oncogene 5:1391-1395. 4. Hale J.E., et al. (1991) J. BioRPB479Hu01 50μg
Recombinant Heparin Binding Epidermal Growth Factor
Like Growth Factor (HBEGF)
Organism Species: Homo sapiens (Human)
Instruction manual
FOR IN VITRO USE AND RESEARCH USE ONLY
NOT FOR USE IN CLINICAL DIAGNOSTIC PROCEDURES
10th Edition (Revised in Jan, 2014)
[ PROPERTIES ]
Residues: Val21~Thr160
Tags: N-terminal His-Tag
Accession: Q99075
Host: E. coli
Subcellular Location: Secreted, extracellular
space. Cell membrane; Single-pass type I
membrane protein. Purity: >95%
Endotoxin Level: <1.0EU per 1μg
(determined by the LAL method).
Formulation: Supplied as lyophilized form in 20mM Tris,
500mM NaCl, pH8.0, containing 1mM EDTA, 1mM DTT,
0.01% sarcosyl, 5% trehalose, and preservative.
Predicted isoelectric point: 9.3
Predicted Molecular Mass: 17.2kDa
Applications: SDS-PAGE; WB; ELISA; IP.
(May be suitable for use in other assays to be determined by the end user.)
[ USAGE ]
Reconstitute in ddH2O. [ STORAGE AND STABILITY ]
Storage: Avoid repeated freeze/thaw cycles.
Store at 2-8oC for one month.
Aliquot and store at -80oC for 12 months.
Stability Test: The thermal stability is described by the loss rate of the target
protein. The loss rate was determined by accelerated thermal degradation test,
that is, incubate the protein at 37oC for 48h, and no obvious degradation and
precipitation were observed. (Referring from China Biological Products Standard,
which was calculated by the Arrhenius equation.) The loss of this protein is less
than 5% within the expiration date under appropriate storage condition.
[ SEQUENCES ]
The sequence of the target protein is listed below.
VTGESLERLR RGLAAGTSNP DPPTVSTDQL LPLGGGRDRK VRDLQEADLD LLRVTLSSKP
QALATPNKEE HGKRKKKGKG LGKKRDPCLR KYKDFCIHGE CKYVKELRAP SCICHPGYHG
ERCHGLSLPV ENRLYTYDHT
[ REFERENCES ]
1. Higashiyama S., et al. (1991) Science 251:936-939.
2. Higashiyama S., et al. (1992) J. Biol. Chem. 267:6205-6212.
3. Mitamura T., et al. (1995) J. Biol. Chem. 270:1015-1019.
4. Elenius K., et al. (1997) EMBO J. 16:1268-1278.. Chem. 266:21145-21149.
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