Search results
1000 results found for “Ephrin”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
CD105 HumanDescription:
Endoglin Human Recombinant
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
Product # :
CYT-525Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Endoglin Human Recombinant extracellular domain produced in E.Coli is a single, glycosylated, Polypeptide containing 151 amino acids (26-176) and having a molecular mass of 43 kDa.The Endoglin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Endoglin solution in 50mM Tris-Acetate, pH-7.5, 1mM EDTA and 20% Glycerol.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities. -
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
-
Physical Appearance
Sterile Filtered colorless liquid formulation.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 43kDa.
What is the source or expression system of CD105 Protein?
Escherichia Coli.
What is the Purity of CD105 Protein?
CD105 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CD105 Protein?
The biological functionality of CD105 Protein will be determined in the future.
What is the amino acid sequence of CD105 Protein?
CD105 Protein is composed from 151amino acids.
What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EGFR AntibodyDescription:
Epidermal Growth Factor Receptor, Mouse Anti Human
Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.
Product # :
ANT-042Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
-
Introduction
The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.
-
Synonyms
Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.
-
Physical Appearance
Sterile filtered colorless solution.
-
Immunogen
Anti-human EGFR mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EGFR amino acids 424-605 purified from E. coli.
-
Ig Subclass
Mouse IgG2b heavy chain and k light chain.
-
Clone
PAT6E3AT.
-
Applications
EGFR antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1000.
Recommended starting dilution is 1:500. -
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
EGFR antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
HERPUD1 HumanDescription:
HERPUD1 Human Recombinant
Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, HERPUD1, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERP, KIAA0025, MIF1, Mif1, SUP.
Product # :
PRO-2105Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
HERPUD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 286 amino acids (1-263) and having a molecular mass of 31.6kDa.HERPUD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HERPUD1 solution (0.5mg/1ml) contains Phosphate buffer saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
HERPUD1 is a multi-pass membrane protein which is a part of the endoplasmic reticulum quality control system. HERPUD1 owns 1 N-terminal ubiquitin-like domain and is expressed highly in the brain. HERPUD1 is also known as ER-associated degradation (ERAD) which takes part in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins.
-
Synonyms
Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, HERPUD1, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERP, KIAA0025, MIF1, Mif1, SUP.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMESETEP EPVTLLVKSP NQRHRDLELS GDRGWSVGHL KAHLSRVYPE RPRPEDQRLI YSGKLLLDHQ CLRDLLPKQE KRHVLHLVCN VKSPSKMPEI NAKVAESTEE PAGSNRGQYP EDSSSDGLRQ REVLRNLSSP GWENISRPEA AQQAFQGLGP GFSGYTPYGW LQLSWFQQIY ARQYYMQYLA ATAASGAFVP PPSAQEIPVV SAPAPAPIHN QFPAENQPAN QNAAPQVVVN PGANQNLRMN AQGGPIVEED DEINRD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NECTIN1 HumanDescription:
Nectin Cell Adhesion Molecule 1 Human Recombinant
PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.
Product # :
PRO-2648Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NECTIN1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 334amino acids (31-355a.a) and having a molecular mass of 37.3kDa.NECTIN1 is fused to an 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The NECTIN1 solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Nectin-1, also referred to as ED4, is a poliovirus receptor- related 1 protein is a part of the Nectin family. Nectin-1 endorses cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions among PVRL1/nectin-1 & PVRL4/nectin-4 and among PVRL1/nectin-1 & PVRL3/nectin-3 have been found. Nectin-1 acts as an entry receptor for herpes simplex virus & pseudorabies virus as well. Likewise, Neurite outgrowth-promoting activity has been shown by Nectin-1.
-
Synonyms
PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
ADPQVVQVND SMYGFIGTDV VLHCSFANPL PSVKITQVTW QKSTNGSKQN VAIYNPSMGV SVLAPYRERV EFLRPSFTDG TIRLSRLELE DEGVYICEFA TFPTGNRESQ LNLTVMAKPT NWIEGTQAVL RAKKGQDDKV LVATCTSANG KPPSVVSWET RLKGEAEYQE IRNPNGTVTV ISRYRLVPSR EAHQQSLACI VNYHMDRFKE SLTLNVQYEP EVTIEGFDGN WYLQRMDVKL
TCKADANPPA TEYHWTTLNG SLPKGVEAQN RTLFFKGPIN YSLAGTYICE ATNPIGTRSG QVEVNITEFP YTPSPPEHGR RAGPVPTAHH HHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IFNAR1 MouseDescription:
Interferon Alpha And Beta Receptor Mouse Recombinant
IFN-R-1, IFN-alpha/beta receptor 1, Type I interferon receptor 1, Ifar, Ifnar, Infar CD118 and Ifnar1.
Product # :
CYT-994Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- SDS-PAGE
Description
IFNAR1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 411 amino acids (27-429a.a) and having a molecular mass of 46.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IFNAR1 is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IFNAR1 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
-
Introduction
Interferon Alpha And Beta Receptor, also known IFNAR1, belongs to the class II cytokine receptor family. IFNAR1 protein forms one of the two chains of a receptor for interferons alpha as well as beta. IFNAR1 binds and activates the receptor which stimulates Janus protein kinases, which in turn phosphorylate some proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also functions as an antiviral factor.
-
Synonyms
IFN-R-1, IFN-alpha/beta receptor 1, Type I interferon receptor 1, Ifar, Ifnar, Infar CD118 and Ifnar1.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
ENLKPPENID VYIIDDNYTL KWSSHGESMG SVTFSAEYRT KDEAKWLKVP ECQHTTTTKC EFSLLDTNVY IKTQFRVRAE EGNSTSSWNE VDPFIPFYTA HMSPPEVRLE AEDKAILVHI SPPGQDGNMW ALEKPSFSYT IRIWQKSSSD KKTINSTYYV EKIPELLPET TYCLEVKAIH PSLKKHSNYS TVQCISTTVA NKMPVPGNLQ VDAQGKSYVL KWDYIASADV LFRAQWLPGY SKSSSGSRSD KWKPIPTCAN VQTTHCVFSQ DTVYTGTFFL HVQASEGNHT SFWSEEKFID SQKHILPPPP VITVTAMSDT LLVYVNCQDS TCDGLNYEII FWENTSNTKI SMEKDGPEFT LKNLQPLTVY CVQARVLFRA LLNKTSNFSE KLCEKTRPGS FSTLEHHHHH H
-
Background
What is the molecular weight/Mw of IFNAR1 MOUSE Protein?
IFNAR1 MOUSE Protein has a total Mw of 46.8kDa.
What is the source or expression system of IFNAR1 MOUSE Protein?
Sf9, Baculovirus cells.
What is the Purity of IFNAR1 MOUSE Protein?
IFNAR1 MOUSE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNAR1 MOUSE Protein?
The biological functionality of IFNAR1 MOUSE Protein will be determined in the future.
What is the amino acid sequence of IFNAR1 MOUSE Protein?
ENLKPPENID VYIIDDNYTL KWSSHGESMG SVTFSAEYRT KDEAKWLKVP ECQHTTTTKC EFSLLDTNVY IKTQFRVRAE EGNSTSSWNE VDPFIPFYTA HMSPPEVRLE AEDKAILVHI SPPGQDGNMW ALEKPSFSYT IRIWQKSSSD KKTINSTYYV EKIPELLPET TYCLEVKAIH PSLKKHSNYS TVQCISTTVA NKMPVPGNLQ VDAQGKSYVL KWDYIASADV LFRAQWLPGY SKSSSGSRSD KWKPIPTCAN VQTTHCVFSQ DTVYTGTFFL HVQASEGNHT SFWSEEKFID SQKHILPPPP VITVTAMSDT LLVYVNCQDS TCDGLNYEII FWENTSNTKI SMEKDGPEFT LKNLQPLTVY CVQARVLFRA LLNKTSNFSE KLCEKTRPGS FSTLEHHHHH H
What applications can IFNAR1 MOUSE Protein be used in?
IFNAR1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNAR1 MOUSE Protein?
The endotoxin level is minimal, IFNAR1 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SRGN Human, HEKDescription:
Serglycin Human Recombinant, HEK
Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.
Product # :
PRO-2046Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Serglycin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Tyr28-Leu158) containing a total of 137 amino acids, having a calculated molecular mass of 15.5kDa and fused to a 6 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
SRGN filtered (0.4µm) solution in phosphate buffered saline and 20% (w/v) glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.
-
Synonyms
Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.
-
Physical Appearance
Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
YPTRRARYQW VRCNPDSNSA NCLEEKGPMF ELLPGESNKI PRLRTDLFPK TRIQDLNRIF PLSEDYSGSG FGSGSGSGSG SGSGFLTEME QDYQLVDESD AFHDNLRSLD RNLPSDSQDL GQHGLEEDFM L HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
C19ORF80 HumanDescription:
Chromosome 19 Open Reading Frame 80 Human Recombinant
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
Product # :
PRO-1575Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
C19ORF80 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 22-198) containing 187 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 21.1kDa (calculated).
Source
Escherichia Coli.
Formulation
C19ORF80 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH-4.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake.
-
Synonyms
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. C19ORF80 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MKHHHHHHASAPMGGPELAQ HEELTLLFHG TLQLGQALNG VYRTTEGRLT KARNSLGLYG RTIELLGQEV SRGRDAAQEL RASLLETQME EDILQLQAEA TAEVLGEVAQ AQKVLRDSVQ RLEVQLRSAW LGPAYREFEV LKAHADKQSH ILWALTGHVQ RQRREMVAQQ HRLRQIQERL HTAALPA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Periostin Human, HEKDescription:
Periostin Human Recombinant, HEK
OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.
Product # :
CYT-835Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Periostin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn22-Gln836) containing a total of 821 amino acids, having a calculated molecular mass of 91.8kDa and fused to a 6 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
Periostin was filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5% trehalose.
Purity
Greater than 38.0% as determined by SDS-PAGE.
More Info
-
Introduction
Periostin is a disulfide linked 90 kDa, 811 amino acid protein originally isolated as a osteoblast-specific factor that functions as a cell adhesion molecule for preosteoblasts and is thought to be involved in osteoblast recruitment, attachment and spreading. Additionally, periostin expression has previously been shown to be significantly increased by both transforming growth factor beta-1(TGFbeta1) and bone morphogenetic protein (BMP-2). OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin
Periostin mRNA is expressed in the developing mouse embryonic and fetal heart, and that it is localized to the endocardial cushions that ultimately divide the primitive heart tube into a four-chambered heart. -
Synonyms
OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Periostin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
NNHYDKILAH SRIRGRDQGP NVCALQQILG TKKKYFSTCK NWYKKSICGQ KTTVLYECCP GYMRMEGMKG CPAVLPIDHV YGTLGIVGAT TTQRYSDASK LREEIEGKGS FTYFAPSNEA WDNLDSDIRR GLESNVNVEL LNALHSHMIN KRMLTKDLKN GMIIPSMYNN LGLFINHYPN GVVTVNCARI IHGNQIATNG VVHVIDRVLT QIGTSIQDFI EAEDDLSSFR AAAITSDILE ALGRDGHFTL FAPTNEAFEK LPRGVLERIM GDKVASEALM KYHILNTLQC SESIMGGAVF ETLEGNTIEI GCDGDSITVN GIKMVNKKDI VTNNGVIHLI DQVLIPDSAK QVIELAGKQQ TTFTDLVAQL GLASALRPDG EYTLLAPVNN AFSDDTLSMD QRLLKLILQN HILKVKVGLN ELYNGQILET IGGKQLRVFV YRTAVCIENS CMEKGSKQGR NGAIHIFREI IKPAEKSLHE KLKQDKRFST FLSLLEAADL KELLTQPGDW TLFVPTNDAF KGMTSEEKEI LIRDKNALQN IILYHLTPGV FIGKGFEPGV TNILKTTQGS KIFLKEVNDT LLVNELKSKE SDIMTTNGVI HVVDKLLYPA DTPVGNDQLL EILNKLIKYI QIKFVRGSTF KEIPVTVYTT KIITKVVEPK IKVIEGSLQP IIKTEGPTLT KVKIEGEPEF RLIKEGETIT EVIHGEPIIK KYTKIIDGVP VEITEKETRE ERIITGPEIK YTRISTGGGE TEETLKKLLQ EEVTKVTKFI EGGDGHLFED EEIKRLLQGD TPVRKLQANK KVQGSRRRLR EGRSQHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin Rat, PEGDescription:
Pegylated Rat Leptin Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-592Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Mono-Pegylated Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus having a molecular mass of 35.6 kDa (with 20 kDa PEG) as determined by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Its half-life in circulation after SC injection was over 20 hours. Rat Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Pegylated Rat Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.More Info
-
Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
-
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized pegylated Rat Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of pegylated Rat Leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Rat leptin can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized pegylated Rat Leptin in sterile water or in sterile 0.4% NaHCO3 adjusted to pH-8.5, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SELE Human, Sf9Description:
E-Selectin Human Recombinant, Sf9
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E
Product # :
PRO-2712Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
SELE Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 541 amino acids (22-556 a.a) and having a molecular mass of 59.4kDa.SELE is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The SELE solution (0.5mg/1ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured by the ability of the immobilized protein to support the adhesion of U937 human histiocytic lymphoma cells, which are added to human E-Seletin/CD62E coated plates 2ug/ml. This effect is > 40%.
More Info
-
Introduction
E-selectin (SELE) is a part of a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. E-selectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.
-
Synonyms
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
WSYNTSTEAM TYDEASAYCQ QRYTHLVAIQ NKEEIEYLNS ILSYSPSYYW IGIRKVNNVW VWVGTQKPLT EEAKNWAPGE PNNRQKDEDC VEIYIKREKD VGMWNDERCS KKKLALCYTA ACTNTSCSGH GECVETINNY TCKCDPGFSG LKCEQIVNCT ALESPEHGSL VCSHPLGNFS YNSSCSISCD RGYLPSSMET MQCMSSGEWS APIPACNVVE CDAVTNPANG FVECFQNPGS FPWNTTCTFD CEEGFELMGA QSLQCTSSGN WDNEKPTCKA VTCRAVRQPQ NGSVRCSHSP AGEFTFKSSC NFTCEEGFML QGPAQVECTT QGQWTQQIPV CEAFQCTALS NPERGYMNCL PSASGSFRYG SSCEFSCEQG FVLKGSKRLQ CGPTGEWDNE KPTCEAVRCD AVHQPPKGLV RCAHSPIGEF TYKSSCAFSC EEGFELHGST QLECTSQGQW TEEVPSCQVV KCSSLAVPGK INMSCSGEPV FGTVCKFACP EGWTLNGSAA RTCGATGHWS GLLPTCEAPT ESNIPHHHHH H
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
FABP3 Human, HisDescription:
Fatty Acid Binding Protein 3 Human Recombinant, His Tag
Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.
Product # :
PRO-668Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
FABP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 19.1 kDa. FABP3 is fused to a 37 amino acid His tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
FABP3 His-Tag is supplied in 20mM Tris-HCl pH 8.0 and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Recombinant Fatty Acid Binding Protein is a newly introduced plasma marker of acute myocardial infarction (AMI). The plasma kinetics of FABP (15kD) closely resemble those of myoglobin in that elevated plasma concentrations are found within 2 hours after AMI and return to normal generally within 18 to 24 hours. But the concentration of FABP in the skeletal muscle is 20 times lower than in cardiac tissue (for myoglobin the same content for cardiac and skeletal tissue), that makes FABP to be more cardiac specific than myoglobin. This makes FABP a useful biochemical marker for the early assessment or exclusion of AMI. FABP also appears to be a useful plasma marker for the estimation of myocardial infarct size.
-
Synonyms
Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.
-
Physical Appearance
Sterile Filtered colorless liquid formulation.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TAC1 HumanDescription:
Tachykinin-1 Human Recombinant
Protachykinin-1, Protachykinin 1, 4930528L02Rik, NK-1, NK1, Nka, Nkna, Neurokinin 2, Neurokinin A, Neurokinin alpha, Neuromedin L, Neuropeptide K, Substance P, Tachykinin precursor 1.
Product # :
PRO-1338Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TAC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (20-129 a.a) and having a molecular mass of 15.6kDa.TAC1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TAC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 2M Urea.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Tachykinin-1 (TAC1) belongs to the tachykinin peptide hormone family. TAC1 are a family of peptides which have similar biologic activities and share a common C-terminal sequence, phe-X-gly-leu-met-NH2, however they have distinct N-terminal sequences that convey receptor specificities. TAC1 is assumed to act as neurotransmitters which interact with nerve receptors and smooth muscle cells. TAC1 induces behavioral responses and serves as vasodilators and secretagogues.
-
Synonyms
Protachykinin-1, Protachykinin 1, 4930528L02Rik, NK-1, NK1, Nka, Nkna, Neurokinin 2, Neurokinin A, Neurokinin alpha, Neuromedin L, Neuropeptide K, Substance P, Tachykinin precursor 1.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMEEIGA NDDLNYWSDW YDSDQIKEEL PEPFEHLLQR IARRPKPQQF FGLMGKRDAD SSIEKQVALL KALYGHGQIS HKRHKTDSFV GLMGKRALNS VAYERSAMQN YERRR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Ferritin Human, FTLDescription:
Ferritin Human Recombinant, Light Chain
Ferritin, FTL, MGC71996, Ferritin light chain.
Product # :
PRO-650Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Ferritin Human Recombinant Light Chain produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20 kDa.
Source
Escherichia Coli.
Formulation
The protein solution (1mg/ml) contains 20mM Tris-HCl pH-7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Ferritin is a fairly large, iron-storage heteropolymeric protein composed of 2 subunit types, light Ferritin & heavy Ferritin polypeptides, which is expressed in most kinds of cells and co-assemble in different proportion in a tissue-specific manner. Ferritin is composed of 24 self-assembled polypeptide subunits of the heavy and light ferritin chains and is characterized by the capacity to remove Fe from solution in the presence of oxygen.
Ferritin light polypeptide protein is the main intracellular iron storage protein in prokaryotes and eukaryotes. Variation in ferritin subunit composition influence the rates of iron uptake and release in various tissues. A key function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in this light chain ferritin gene are associated with several neurodegenerative diseases and hyper ferrit anemia-cataract syndrome.
Ferritin stores iron in a soluble, nontoxic, readily accessible form. Ferritin is needed for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after it has been oxidized. -
Synonyms
Ferritin, FTL, MGC71996, Ferritin light chain.
-
Physical Appearance
Sterile Filtered solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MSSQIRQNYS TDVEAAVNSL VNLYLQASYT YLSLGFYFDR DDVALEGVSH FFRELAEEKR EGYERLLKMQ NQRGGRALFQ DIKKPAEDEW GKTPDAMKAA MALEKKLNQA LLDLHALGSA RTDPHLCDFL ETHFLDEEVK LIKKMGDHLT NLHRLGGPEA GLGEYLFERL TLKHD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PFN1 HumanDescription:
Profilin-1 Human Recombinant
Profilin-1, Profilin I, PFN1.
Product # :
PRO-528Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PFN1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 140 amino acids (1-140 a.a.) and having a molecular mass of 15kDa.The PFN1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PFN1 protein solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Profilin1 (PFN1) is a ubiquitous actin monomer-binding protein which is a member of the profilin family. PFN1 significantly boosts skin wound healing in-vitro and in-vivo which may be mediated by purinergic receptors. PFN1 is also active in endothelial cell migration and vessel sprouting. PFN1 is thought to control actin polymerization in response to extracellular signals. PFN1 binds to actin and affects the formation of the cytoskeleton. In addition, PFN1 has an important role in the regulation of epithelial cell-cell adhesion. At high concentrations, profilin averts the polymerization of actin, while at low concentrations it enhances the polymerization. PFN1 gene deletion is linked to Miller-Dieker syndrome.
-
Synonyms
Profilin-1, Profilin I, PFN1.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MAGWNAYIDN LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VNITPAEVGV LVGKDRSSFY VNGLTLGGQK CSVIRDSLLQ DGEFSMDLRT KSTGGAPTFN VTVTKTDKTL VLLMGKEGVH GGLINKKCYE MASHLRRSQY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
FTH1 HumanDescription:
Ferritin Human Recombinant, Heavy Chain
Ferritin heavy chain, Cell proliferation-inducing gene 15 protein, FTH1, FHC, FTH, PLIF, FTHL6, PIG15, MGC104426.
Product # :
PRO-658Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
FTH1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids and having a molecular mass of 21 kDa.
Source
Escherichia Coli.
Formulation
The FTH1 protein solution contains 20mM Tris-HCl pH-7.5, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Ferritin is a fairly large, iron-storage heteropolymeric protein composed of 2 subunit types, light Ferritin & heavy Ferritin polypeptides, which is expressed in most kinds of cells and co-assemble in different proportion in a tissue-specific manner. Ferritin is composed of 24 self-assembled polypeptide subunits of the heavy and light ferritin chains and is characterized by the capacity to remove Fe (II) from solution in the presence of oxygen.
Ferritin light polypeptide protein is the main intracellular iron storage protein in prokaryotes and eukaryotes. Variation in ferritin subunit composition influence the rates of iron uptake and release in various tissues. A key function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in this light chain ferritin gene are associated with several neurodegenerative diseases and hyper ferrit anemia-cataract syndrome.
Ferritin stores iron in a soluble, nontoxic, readily accessible form. Ferritin is needed for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after it has been oxidized. -
Synonyms
Ferritin heavy chain, Cell proliferation-inducing gene 15 protein, FTH1, FHC, FTH, PLIF, FTHL6, PIG15, MGC104426.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MTTASTSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK NFAKYFLHQS HEEREHAEKL MKLQNQRGGR IFLQDIKKPD CDDWESGLNA MECALHLEKN VNQSLLELHK LATDKNDPHL CDFIETHYLN EQVKAIKELG DHVTNLRKMG APESGLAEYL FDKHTLGDSD NES.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Adiponectin (108-244) HumanDescription:
Adiponectin (108-244 a.a.) Human Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-073Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page
Description
Acrp30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (108-244 a.a.) and having a molecular mass of 18.1kDa.Acrp30 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Acrp30 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
sds-page
More Info
-
Introduction
Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.
-
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN.
-
Background
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 18.1kDa.What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein? MGSSHHHHHH SSGLVPRGSH MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN..
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN Protein was purified using conventional chromatography techniques
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin tA Mouse, PEGDescription:
Leptin Antagonist Triple Mutant Pegylated Mouse Recombinant
Product # :
CYT-566Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.The Mouse Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Mouse Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Leptin Antagonist Triple Mutant Mouse Recombinant half-life in circulation after SC injection was over 20 hours.
Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Mouse Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
-
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EDAR AntibodyDescription:
Ectodysplasin A Receptor, Mouse Anti Human
Ectodysplasin A Receptor, DL, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Ectodysplasin-A Receptor, Downless Homolog, EDA-A1 Receptor, ECTD10A, ECTD10B, EDA3, HRM1, ED3, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, EDA-A1R, EDA1R, ED1R, ED5, Tumor necrosis factor receptor superfamily member EDAR.
Product # :
ANT-560Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
Ectodysplasin A Receptor, also known as EDAR belongs to the tumor necrosis factor receptor family. EDAR is a receptor for the soluble ligand ectodysplasin A, and is capable of activating the nuclear factor-kappaB, JNK, as well as caspase-independent cell death pathways. EDAR is necessary for the development of hair, teeth, and other ectodermal derivatives. Furthermore, mutations in EDAR resulted in autosomal dominant and recessive forms of hypohidrotic ectodermal dysplasia.
-
Synonyms
Ectodysplasin A Receptor, DL, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Ectodysplasin-A Receptor, Downless Homolog, EDA-A1 Receptor, ECTD10A, ECTD10B, EDA3, HRM1, ED3, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, EDA-A1R, EDA1R, ED1R, ED5, Tumor necrosis factor receptor superfamily member EDAR.
-
Physical Appearance
Sterile filtered colorless solution.
-
Immunogen
Anti-human EDAR mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human EDAR protein 27-448 amino acids purified from E. coli.
-
Ig Subclass
Mouse IgG2a heavy chain and k light chain.
-
Clone
PAT19E8AT.
-
Applications
EDAR antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
EDAR antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CST3 Mouse, ActiveDescription:
Cystatin-C Mouse Recombinant, Active
Cystatin-C, Cystatin-3, Cst3, CST3
Product # :
PRO-2433Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CST3 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 126 amino acids (21-140 a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).CST3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CST3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The IC50 value is < 1.0nM. The inhibitory function of Cystatin 3 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25°C.
More Info
-
Introduction
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.
-
Synonyms
Cystatin-C, Cystatin-3, Cst3, CST3
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
ATPKQGPRML GAPEEADANE EGVRRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL TDCPFHDQPH LMRKALCSFQ IYSVPWKGTH SLTKFSCKNA HHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EGF Human, PichiaDescription:
Epidermal Growth Factor Human Recombinant, Pichia
Urogastrone, URG, EGF.
Product # :
CYT-332Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Epidermal Growth Factor Human Recombinant produced in Pichia Pastoris is a single, glycosylated, polypeptide chain containing 51 amino acids and having a molecular mass of 6KDa.The EGF is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
Lyophilized from a filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED₅₀, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 107 Units/mg.
More Info
-
Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
-
Synonyms
Urogastrone, URG, EGF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.
-
Background
Harnessing Pichia for Epidermal Growth Factor Human Recombinant Production: Novel Approaches and Therapeutic Implications
Abstract:
This research paper delves into a cutting-edge avenue of Epidermal Growth Factor (EGF) Human Recombinant production by leveraging Pichia as an expression host. Through a synthesis of advanced methodologies encompassing genetic engineering, fermentation, and bioinformatics, this study explores the potential of Pichia-based platforms for enhanced EGF yield and biological activity. The findings not only offer insights into efficient EGF production but also underscore the therapeutic prospects of this approach.
Introduction:
Epidermal Growth Factor (EGF) holds a crucial place in cellular processes. This paper explores a novel dimension of EGF Human Recombinant production utilizing Pichia expression systems, emphasizing both technical aspects and the potential impact on therapeutic applications.
Pichia as an Expression Host:
Pichia stands as a promising alternative to conventional expression platforms due to its robustness and eukaryotic machinery. This paper investigates the strategic integration of EGF gene into Pichia, utilizing tailored vectors and promoters for optimal protein production.
Genetic Engineering Strategies:
Precise genetic manipulation is pivotal for enhanced EGF yield. Gene codon optimization and signal peptide selection are meticulously undertaken to ensure proper protein folding and secretion in Pichia. Through these approaches, EGF expression and secretion are finely tuned, resulting in biologically active EGF.
Fermentation and Protein Purification:
Expression is followed by fermentation in controlled conditions, leading to EGF accumulation. This step is supplemented by purification processes like chromatography, ensuring high EGF purity. Biochemical assays validate the biological activity of the purified EGF, affirming its therapeutic potential.
Bioinformatics in EGF-Pichia Interaction:
Advanced bioinformatics analyses shed light on the intricate interactions between EGF and Pichia host. Structural modeling and molecular dynamics simulations provide insights into potential post-translational modifications and protein-protein interactions, enriching our understanding of EGF behavior in Pichia.
Therapeutic Implications:
Beyond production, the paper emphasizes the therapeutic significance of EGF produced in Pichia. Enhanced production efficiency directly impacts cost-effectiveness, broadening its accessibility for therapeutic use. The EGF-Pichia approach presents exciting avenues for wound healing therapies and targeted cancer interventions.
Challenges and Future Directions:
Despite the progress, challenges such as glycosylation patterns and scaling-up strategies remain. Future efforts should focus on refining glycosylation profiles to ensure consistent bioactivity and optimizing bioreactor designs to scale up production for clinical applications.
Conclusion:
In a synergy of advanced methodologies and therapeutic implications, the Pichia-based Epidermal Growth Factor Human Recombinant production presents an innovative paradigm. The intricate harmony between Pichia host and EGF production holds promise for novel therapies, underscoring the potential impact of this pioneering approach.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6kDa.
What is the source or expression system of EGF Protein?
Pichia Pastoris.
What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF Protein?
The ED₅₀, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 107 Units/mg.
What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ESAT6-CFP10Description:
ESAT6-CFP10 Chimeric Recombinant
Early Secretory Target Mycobacterium Tuberculosis, ESAT-6
Product # :
PRO-2737Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Chimeric ESAT6-CFP10 produced in E. coli is fused to a 6 amino acid his tag at its C-terminus and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
ESAT6-CFP10 solution contains 25mM K2CO3, 0.02% NaN3 and PBS.
Purity
Protein is >95% pure as determined by 12% PAGE (coomassie staining).
More Info
-
Introduction
Mycobacterium antigen ESAT6 has been isolated from low molecular weight fractions of the shot-term-culture filtrate (ST-CF) and it can easily be detected in tuberculosis patients. The export of ESAT-6 which is a potent T-cell antigen, and related proteins requires a dedicated secretory apparatus that is encoded by a group of genes, several of which also code for proteins that are recognized strongly by T cells. The ESAT-6 systems can consequently be considered as immunogenicity islands and there is mounting evidence that the equivalent genes are subject to selective pressure imposed by the immune system of the host. This antigen includes many epitopes detectable in the serum of most patients with tuberculosis (more than 90%). By the attempts to obtain the vaccine on the basis of ESAT-6 it was demonstrated that the optimization of adjuvant is very important when using the combination of dioctadecylammonium bromide and monophosphoryllipide. ESAT-6 is very potential as diagnostic for differentiation between the mycobacterial infection and BCG vaccination. The main topic in ESAT-6 using is in antibody production and in test-systems for tuberculosis elaboration. Early secretory antigen 6 (ESAT6) and cell filtrate protein 10 (CFP10) are 2 antigens secreted as a complex by the replicating Mycobacterium tuberculosis complex (MTC).
-
Synonyms
Early Secretory Target Mycobacterium Tuberculosis, ESAT-6
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Applications
Immunoassay.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
VEGF HumanDescription:
Vascular Endothelial Growth Factor Human Recombinant
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-241Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Vascular Endothelial Growth Factor Human Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38.2kDa.The VEGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The VEGF protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 3.7-5.6 ng/ml, corresponding to a Specific Activity of 178,570-270,270IU/mg.More Info
-
Introduction
Vascular endothelial growth factor (VEGF) is an important signaling protein involved in vessel formation As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ). VEGF mediates increased vascular permeability, induces vasculogenesis and endothelial cell production, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor. VEGF is located in normal cartilage though only osteoarthritic cartilage expresses the VEGF receptors, NP1, VEGFR1 and VEGFR2. The VEGF level in the culture media from OA chondrocytes was more than 3 folds higher than in media from normal chondrocytes
-
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized VEGF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR
-
Protein content
VEGF protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.2875 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of VEGF as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin qA Ovine, PEGDescription:
Leptin Quadruple Antagonist Pegylated Ovine Recombinant
Product # :
CYT-1246Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Ovine Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Ovine Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Ovine Leptin Quadruple anatagonist Pegylated runs as a 48 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Ovine Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Pegylated Ovine Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant Ovine leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super Ovine leptin antagonist but is 15 fold higher as compared to pegylated recombinant super active ovine leptin antagonist.
More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
-
Background
Leptin is mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mostly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor can be found on a various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which save energy. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
-
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GoserelinDescription:
Goserelin
Product # :
HOR-256Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Goserelin contains 10 amino acids Glu1-His2-Trp3-Ser4-Tyr5-D-Ser(tBu)6-Leu7-Arg8-Pro9-AzGly10-NH2 and having a molecular weight of 1269.43 Dalton.
Formulation
The Goserelin peptide was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Goserelin is a hormone similar to the one normally released from the hypothalamus gland in the brain (GnRH super-agonist). It is used to treat for prostate and breast cancer.
Goserelin decreases the amount of estrogen and testosterone by this treating endometriosis and cancer of the breast, and can help thin the uterus lining before surgery. Goserelin prevents the growth of tissue associated with endometriosis.
Reducing the amount of testosterone is one way of treating prostate cancer. -
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Goserelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Goserelin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Goserelin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.