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1000 results found for “secretogranin”
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Name :
Ag85ADescription:
Mycobacterium Tuberculosis major secretory protein Antigen 85A Recombinant
Ronectin-binding protein A, Mycolyl transferase 85A.
Product # :
PRO-1076Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Mycobacterium tuberculosis Ag85A (43-338 a.a) produced in Hi-5 cells is a single, glycosylated polypeptide chain having a molecular mass of 32.8kDa (305 a.a in total).Antigen 85A is fused to a 6 amino acid His tag at C-terminus and purified by conventional chromatographic techniques.
Source
Baculovirus
Formulation
The Ag85A solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Antigen 85A is a member of the antigen 85 complex (Antigen 85A, B, C). The enzymes of the antigen 85 complex have mycolyltransferase activity and catalyze the synthesis of the very rich glycolipid of the mycobacterial cell wall, the cord factor (trehalose 6,6'-dimycolate, TDM). The cord factor is vital for the integrity of the mycobacterial cell wall and pathogenesis of the bacillus. TDM is synthesized from two molecules of trehalose-6'-monomycolate (TMM) by Antigen 85A.
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Synonyms
Ronectin-binding protein A, Mycolyl transferase 85A.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADPAFSRPGL PVEYLQVPSP SMGRDIKVQF QSGGANSPAL YLLDGLRAQD DFSGWDINTP AFEWYDQSGL SVVMPVGGQS SFYSDWYQPA CGKAGCQTYK WETFLTSELP GWLQANRHVK PTGSAVVGLS MAASSALTLA IYHPQQFVYA GAMSGLLDPS QAMGPTLIGL AMGDAGGYKA SDMWGPKEDP AWQRNDPLLN VGKLIANNTR VWVYCGNGKP SDLGGNNLPA KFLEGFVRTS NIKFQDAYNA GGGHNGVFDF PDSGTHSWEY WGAQLNAMKP DLQRALGATP NTGPAPQGAH HHHHH.
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.
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Name :
SELE Human, HEKDescription:
E-Selectin Human Recombinant, HEK
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-1645Price :
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Shipped at Room temp
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Description
SELE Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 543 amino acids (22-556). SELE is fused to an 8 amino acid His-tag at C-terminus is purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
SELE was lyophilized from a 0.2 µM filtered solution of PBS and 4% Mannitol, pH 7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin 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.
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Synonyms
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SELE although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SELE should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized SELE in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
WSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILSYSPSYYWIGIRKVNNVW
VWVGTQKPLTEEAKNWAPGEPNNRQKDEDCVEIYIKREKDVGMWNDERCSKKKLALCYTA
ACTNTSCSGHGECVETINNYTCKCDPGFSGLKCEQIVNCTALESPEHGSLVCSHPLGNFSY
NSSCSISCDRGYLPSSMETMQCMSSGEWSAPIPACNVVECDAVTNPANGFVECFQNPGSFPW
NTTCTFDCEEGFELMGAQSLQCTSSGNWDNEKPTCKAVTCRAVRQPQNGSVRCSHSPAGEFT
FKSSCNFTCEEGFMLQGPAQVECTTQGQWTQQIPVCEAFQCTALSNPERGYMNCLPSASGSFR
YGSSCEFSCEQGFVLKGSKRLQCGPTGEWDNEKPTCEAVRCDAVHQPPKGLVRCAHSPIGEFTY
KSSCAFSCEEGFELHGSTQLECTSQGQWTEEVPSCQVVKCSSLAVPGKINMSCSGEPVFGTVCKF
ACPEGWTLNGSAARTCGATGHWSGLLPTCEAPTESNIPVDHHHHHH.
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 :
PDPN HumanDescription:
Podoplanin Human Recombinant
Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.
Product # :
PRO-626Price :
Quantity :
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Shipped with Ice Packs
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Description
PDPN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (99-207 a.a) and having a molecular mass of 13.4kDa. PDPN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris-HCl pH7.5 & 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Podoplanin is a small mucin-like type-1 transmembrane protein, typically expressed in various specialized cell types throughout the body. Podoplanin is a type-I integral membrane glycoprotein with diverse distribution in human tissues. PDPN physiological function is related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor.
PDPN is expressed in lymphatic progenitor cells and afterwards during mouse development in lymphatic endothelial cells. Podoplanin is a specific marker for lymph vessel endothelial cells. Over-expression of podoplanin significantly elevates endothelial cell adhesion, migration, and tube formation. Inhibition of Podoplanin expression decreases cell adhesion in human dermal lymphatic endothelial cells. Podoplanin is used as a specific marker for lymphatic endothelium in histopathology.
Podoplanin expression is increased in nearly all human colon, rectum, and small intestine tumors. AGGRUS may serve as a diagnostic marker that distinguishes seminomas, the majority of which over express the protein, from embryonal carcinoma in testicular germ cell tumors. -
Synonyms
Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASTGQPEDD TETTGLEGGV AMPGAEDDVV TPGTSEDRYK SGLTTLVATS VNSVTGIRIE DLPTSESTVH AQEQSPSATA SNVATSHSTE KVDGDTQTTV EKDGLSTVTL.
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 :
OTOR HumanDescription:
Otoraplin Human Recombinant
Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.
Product # :
CYT-582Price :
Quantity :
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Shipped at Room temp
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Description
Otoraplin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.7 kDa.The OTOR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OTOR protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM NaCl.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness. -
Synonyms
Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized OTOR Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OTOR 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.
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Solubility
It is recommended to reconstitute the lyophilized Otoraplin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VHGIFMDRLASKKLCADDECVYTISLASAQEDYNAPDCRFINVKKGQQIYVYS
KLVKENGAGEFWAGSVYGDGQDEMGVVGYFPRNLVKEQRVYQEATKEVPTT
DIDFFCE.
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.
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Name :
TAGLN HumanDescription:
Transgelin Human Recombinant
SM22, SMCC, TAGLN1, WS3-10, Transgelin, Smooth muscle protein 22-alpha, SM22-alpha, TAGLN, DKFZp686B01212, DKFZp686P11128.
Product # :
PRO-851Price :
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Shipped with Ice Packs
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Description
TAGLN Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-201 a.a.) and having a molecular mass of 24.8 kDa. The TAGLN is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TAGLN Human solution containing 20mM Tris-HCl pH-7.5, 1mM DTT & 20% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
TAGLN is a transformation and form-change responsive actin cross-linking/gelling protein that is part of the calponin family. TAGLN is expressed abundantly in fibroblasts and smooth muscle. TAGLN participates in calcium interactions and contractile properties of the cell that contribute to replicative senescence. Throughout embryogenesis, TAGLN is expressed in smooth, cardiac and skeletal muscle, but is limited during late fetal growth and adulthood to all vascular and visceral smooth muscle cells and low levels of expression in heart. TAGLN is downregulated in several transformed cell lines, showing that a decrease of TAGLN expression is an premature indicator of the onset of transformation.
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Synonyms
SM22, SMCC, TAGLN1, WS3-10, Transgelin, Smooth muscle protein 22-alpha, SM22-alpha, TAGLN, DKFZp686B01212, DKFZp686P11128.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MANKGPSYGM SREVQSKIEK KYDEELEERL VEWIIVQCGP DVGRPDRGRL GFQVWLKNGV ILSKLVNSLY PDGSKPVKVP ENPPSMVFKQ MEQVAQFLKA AEDYGVIKTD MFQTVDLFEG KDMAAVQRTL MALGSLAVTK NDGHYRGDPN WFMKKAQEHK REFTESQLQE GKHVIGLQMG SNRGASQAGM TGYGRPRQII S.
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.
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Name :
ASRGL1 HumanDescription:
ASRGL1 Human Recombinant
ALP, ALP1, CRASH, ,Beta-aspartyl-peptidase, Isoaspartyl dipeptidase.
Product # :
ENZ-837Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ASRGL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-308 a.a) and having a molecular mass of 34.4kDa.ASRGL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ASRGL1 protein solution (0.5mg/ml) containing Phosphate buffer saline, (pH 7.4) ,10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ASRGL1 is a 308 amino acid protein which is a member of the Ntn-hydrolase family. ASRGL1 is an autoantigenic protein which is present in the mid-piece of sperm after obstruction of the male reproductive tract. ASRGL1 is expressed highly in the testis, but is also expressed in the brain, kidney and gastrointestinal tissues. High levels of ASRGL1 are also detected in ovarian, uterine and mammary tumors in comparison with normal tissues of the same origin.
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Synonyms
ALP, ALP1, CRASH, ,Beta-aspartyl-peptidase, Isoaspartyl dipeptidase.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNPIVVV HGGGAGPISK DRKERVHQGM VRAATVGYGI LREGGSAVDA VEGAVVALED DPEFNAGCGS VLNTNGEVEM DASIMDGKDL SAGAVSAVQC IANPIKLARL VMEKTPHCFL TDQGAAQFAA AMGVPEIPGE KLVTERNKKR LEKEKHEKGA QKTDCQKNLG TVGAVALDCK GNVAYATSTG GIVNKMVGRV GDSPCLGAGG YADNDIGAVS TTGHGESILK VNLARLTLFH IEQGKTVEEA ADLSLGYMKS RVKGLGGLIV VSKTGDWVAK WTSTSMPWAA AKDGKLHFGI DPDDTTITDL P.
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.
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Name :
Betacellulin His HumanDescription:
Betacellulin Human Recombinant, His Tag
Betacellulin, Probetacellulin.
Product # :
CYT-077Price :
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Shipped with Ice Packs
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- sds-page
Description
BTC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (32-111) and having a molecular mass of 11.3 kDa.BTC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The BTC solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 0.2M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
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Synonyms
Betacellulin, Probetacellulin.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y
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Background
What is the molecular weight/Mw of BETACELLULIN Protein?
BETACELLULIN Protein has a total Mw of 11.3kDa.
What is the source or expression system of BETACELLULIN Protein?
Escherichia Coli.
What is the Purity of BETACELLULIN Protein?
BETACELLULIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of BETACELLULIN Protein?
The biological functionality of BETACELLULIN Protein will be determined in the future.
What is the amino acid sequence of BETACELLULIN Protein?
MGSSHHHHHH SSGLVPRGSH MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y
What applications can BETACELLULIN Protein be used in?
BETACELLULIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BETACELLULIN Protein?
The endotoxin level is minimal, BETACELLULIN 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 :
EREG HumanDescription:
Epiregulin Human Recombinant
EREG, Epiregulin, ER.
Product # :
CYT-609Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Epiregulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 49 amino acids and having a molecular mass of 5.6 kDa. Epiregulin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Epiregulin was lyophilized from 0.5mg/ml solution ciontaing 20mM PBS buffer pH-7.4 containing 20mM sodium chloride.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.More Info
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Introduction
Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.
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Synonyms
EREG, Epiregulin, ER.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Epiregulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Epiregulin 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.
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Solubility
It is recommended to reconstitute the lyophilized Epiregulin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.
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Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 5.6kDa.
What is the source or expression system of EREG Protein?
Escherichia Coli.
What is the Purity of EREG Protein?
EREG Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.
What is the amino acid sequence of EREG Protein?
VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.
What applications can EREG Protein be used in?
EREG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EREG Protein?
The endotoxin level is minimal, EREG 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.
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Name :
TRIM21 Human BiotinDescription:
Tripartite Motif Containing 21 (RO52) Human Recombinant, Biotinylated
52 kDa Ro protein, Sjoegren syndrome type A antigen, SS-A, Ro(SS-A), 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Tripartite motif-containing protein 21, RING finger protein 81, TRIM21, RNF81, RO52, SSA1, SSA, RO-52.
Product # :
PRO-2559Price :
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Description
TRIM21 Human Recombinant, Biotin produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 52kDa. TRIM21 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
TRIM21 solution is supplied in 20mM HEPES pH-7.6, 0.01mM EDTA and 0.02% SDS.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
TRIM21 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The 52 kDa Ro protein is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. Ro/SSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus. Ribonucleoprotein particle is composed of a single polypeptide and one of four small RNA molecules. The RoSSA is present in all mammalian cells studied but has no known function. At least 2 isoforms are present in nucleated and red blood cells, and tissue specific differences in Ro/SSA proteins were identified.
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Synonyms
52 kDa Ro protein, Sjoegren syndrome type A antigen, SS-A, Ro(SS-A), 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Tripartite motif-containing protein 21, RING finger protein 81, TRIM21, RNF81, RO52, SSA1, SSA, RO-52.
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Physical Appearance
Sterile Filtered clear solution.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG type human auto antibodies.2. Functional Streptavidin based ELISA test (analysis of positive/negative samples.)
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.
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Name :
GAL HumanDescription:
Galanin Prepropeptide Human Recombinant
GALN, GLNN, GMAP, GAL, GAL1.
Product # :
PRO-1433Price :
Quantity :
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Shipped with Ice Packs
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Description
GAL Human Recombinant produced in E. coli is a single polypeptide chain containing 127 amino acids (20-123) and having a molecular mass of 13.9kDa. GAL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GAL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Galanin Prepropeptide (GAL) which is localized in brain pathways is involved in both cognition and affect, and also inhibits learning and memory by inhibiting neurotransmitter release and neuronal firing rate. GAL is a part of the galanin family and modulates a variety of physiological processed including cognition/memory, sensory/pain processing, neurotransmitter/hormone secretion, and feeding behavior. Galanin Prepropeptide is upregulated in primary afferent and sympathetic neurones and is required for the development of sympathetic perineuronal baskets subsequent to nerve injury.
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Synonyms
GALN, GLNN, GMAP, GAL, GAL1.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSASAGLWS PAKEKRGWTL NSAGYLLGPH AVGNHRSFSD KNGLTSKREL RPEDDMKPGS FDRSIPENNI MRTIIEFLSF LHLKEAGALD RLLDLPAAASSEDIERS.
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.
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Name :
SEPT3 HumanDescription:
Septin-3 Human Recombinant
Septin 3, SEP3, Neuronal-Specific Septin 3, Neuronal-Specific Septin-3, BK250D10.3, Neuronal-specific septin-3.
Product # :
PRO-2152Price :
Quantity :
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Shipped with Ice Packs
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Description
SEPT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-358 a.a) and having a molecular mass of 43.1kDa. SEPT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SEPT3 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Septin-3, also known as SEPT3 is a member of the septin family of GTPases. Members of this family are essential for cytokinesis. Furthermore, expression is up regulated by retinoic acid in a human teratocarcinoma cell line. The exact role of SEPT3 has not been determined yet. In addition, among its related pathways are Bacterial invasion of epithelial cells.
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Synonyms
Septin 3, SEP3, Neuronal-Specific Septin 3, Neuronal-Specific Septin-3, BK250D10.3, Neuronal-specific septin-3.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSKGLPE TRTDAAMSEL VPEPRPKPAV PMKPMSINSN LLGYIGIDTI IEQMRKKTMK TGFDFNIMVV GQSGLGKSTL VNTLFKSQVS RKASSWNREE KIPKTVEIKA IGHVIEEGGV KMKLTVIDTP GFGDQINNEN CWEPIEKYIN EQYEKFLKEE VNIARKKRIP DTRVHCCLYF ISPTGHSLRP LDLEFMKHLS KVVNIIPVIA KADTMTLEEK SEFKQRVRKE LEVNGIEFYP QKEFDEDLED KTENDKIRQE SMPFAVVGSD KEYQVNGKRV LGRKTPWGII EVENLNHCEF ALLRDFVIRT HLQDLKEVTH NIHYETYRAK RLNDNGGLPP GEGLLGTVLP PVPATPCPTA E.
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 :
GLP 1 HumanDescription:
Human Glucagon Like Peptide-1
GLP1, Glucagon Like Peptide-1, Incretin hormone.
Product # :
HOR-284Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
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Description
Glucagon Like Peptide-1 is a single, non-glycosylated, polypeptide chain containing 30 amino acids and having a molecular mass of 3297.7 Dalton.The GLP-1 is purified by proprietary chromatographic techniques.
Formulation
The GLP-1 peptide was lyophilized with no additives.
Purity
Greater than 96.0% as determined by RP-HPLC.
More Info
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Introduction
Glucagon-like peptide-1 (GLP-1) is derived from the transcription product of the proglucagon gene. The major source of GLP-1 in the body is the intestinal L cell that secretes GLP-1 as a guthormone. The biologically active forms of GLP-1 are: GLP-1-(7-37) and GLP-1-(7-36)NH2.
GLP-1 secretion by L cells is dependent on the presence of nutrients in the lumen of the small intestine. The secretagogues (agents that causes or stimulates secretion) of this hormone include major nutrients like carbohydrate, proteinand lipid. Once in the circulation, GLP-1 has a half life of less than 2 minutes, due to rapid degradation by the enzyme dipeptidyl peptidase-4.
GLP-1 possesses several physiological properties that make it a subject of intensive investigation as a potential treatment of diabetes mellitus. The known physiological functions of GLP-1 include: Increases insulin secretion from the pancreas in a glucose-dependent manner, decreases glucagon secretion from the pancreas, increases beta cells mass and insulin gene expression, inhibits acid secretion and gastric emptying in the stomach, decreases food intake by increasing satiety. -
Synonyms
GLP1, Glucagon Like Peptide-1, Incretin hormone.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Glucagon Like Peptide-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GLP-1 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.
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Solubility
It is recommended to reconstitute the lyophilized Glucagon Like Peptide-1 in sterile H2O at 0.5mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
H-His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Lys-Glu-Phe-Ile-Ala-Trp-Leu-Val-Lys-Gly-Arg-NH2.
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 :
SEPT2 HumanDescription:
Septin-2 Human Recombinant
Septin 2, DIFF6, NEDD5, hNedd5, Pnutl3, NEDD-5.
Product # :
PRO-255Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SEPT2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 381 amino acids (1-361 a.a.) and having a molecular mass of 43.6kDa. SEPT2 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SEPT2 solution (0.25mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SEPT2 is a GTPase which is mandatory for cytokinesis and related to exocytosis. Septin-2 protein is able to hetero-oligomerize with Septin6, 7 and in addition takes part in the organization of new growth in organisms. SEPT2 is associated with a Tau-based paired helical filament core and contributes to the creation of neurofibrillary tangle as integral constituents of paired helical filaments.
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Synonyms
Septin 2, DIFF6, NEDD5, hNedd5, Pnutl3, NEDD-5.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK STLINSLFLT DLYPERVISG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV DTPGYGDAIN CRDCFKTIIS YIDEQFERYL HDESGLNRRH IIDNRVHCCF YFISPFGHGL KPLDVAFMKA IHNKVNIVPV IAKADTLTLK ERERLKKRIL DEIEEHNIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV GSNQLIEAKG KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG DGDGGALGHH V.
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 :
HexarelinDescription:
Hexarelin
Product # :
HOR-288Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Hexarelin has 7 amino acids H-His-D-2-Methyl-Trp-Ala-Trp-D-Phe-Lys-NH2 and having a molecular weight of 887 Dalton. The Molecular Formula is C47H58N12O6.
Formulation
The Hexarelin 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
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Introduction
Hexarelin stimulates GH secretion. Hexarelin is more resistant to proteolytic degradation than GHRP-6.
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Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
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Stability
Lyophilized Hexarelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Hexarelin 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.
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Solubility
It is recommended to reconstitute the lyophilized Hexarelin 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.
- View Data Sheet
Name :
SHBG ProteinDescription:
Sex Hormone-Binding Globulin Human
Sex hormone-binding globulin, SHBG, Sex steroid-binding protein, SBP, Testis-specific androgen-binding protein, ABP, Testosterone-estradiol-binding globulin, TeBG, Testosterone-estrogen-binding globulin, SHBG.
Product # :
PRO-2757Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SHBG is a protein of approximately 45kD.
Source
Human serum.
Formulation
The protein is supplied in 0.01M HEPES, PH 7.4 and 0.15M NaCl.
More Info
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Introduction
Sex-hormone-binding globulin (SHBG) is a beta-globulin which specifically binds steroid hormones; it is involved in the transport of sex steroids in plasma. The main site of SHBG synthesis is assumed to be the hepatocytes. The production of SHBG is regulated by androgen/estrogen balance, thyroid hormones, insulin and dietary factors, among others. The concentration of SHBG is a key factor regulating their distribution between protein-bound and free states. SHBG concentration determination is primarily significant in the evaluation of mild disorders of androgen metabolism and it allows detection of women with hirsutism who are likely to react to estrogen therapy. Testosterone/SHBG-ratios correlate well with both measured and calculated values for free testosterone thus aid to distinguish between subjects with excessive androgen activity and normal individuals. SHBG gene polymorphisms are linked with polycystic ovary syndrome and type 2 diabetes mellitus.
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Synonyms
Sex hormone-binding globulin, SHBG, Sex steroid-binding protein, SBP, Testis-specific androgen-binding protein, ABP, Testosterone-estradiol-binding globulin, TeBG, Testosterone-estrogen-binding globulin, SHBG.
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Physical Appearance
Streile filtered colorless solution.
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Stability
Upon arrival, Store at -20°C. Please prevent freeze-thaw cycles.
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Human Virus Test
FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, Parvovirus B19, HBc, HBV, HIV and Syphilis.
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 :
SEPSECS HumanDescription:
Selenocysteinyl-tRNA(Sec) synthase Human Recombinant
SLA, SLA/LP autoantigen, SLA-p35, Selenocysteinyl-tRNA(Sec) synthase, Selenocysteine synthase, Liver-pancreas antigen, Soluble liver antigen, Sec synthase, UGA suppressor tRNA-associated protein.
Product # :
ENZ-033Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SEPSECS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 521 amino acids (1-501a.a.) and having a molecular mass of 57.9kDa.SEPSECS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SEPSECS protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 1mM DTT, 100mM NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SEPSECS catalyzes the last step of sec synthesis by way of converting O-phosphoseryl-tRNA(sec) to selenocysteinyl-tRNA(sec) using selenophosphate as the selenium donor. Furthermore, SEPSECS protein is considered a specific marker of autoimmune hepatitis.
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Synonyms
SLA, SLA/LP autoantigen, SLA-p35, Selenocysteinyl-tRNA(Sec) synthase, Selenocysteine synthase, Liver-pancreas antigen, Soluble liver antigen, Sec synthase, UGA suppressor tRNA-associated protein.
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Physical Appearance
Sterile Filtered clear solution.
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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
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNRESFAAGE RLVSPAYVRQ GCEARRSHEH LIRLLLEKGK CPENGWDEST LELFLHELAI MDSNNFLGNC GVGEREGRVA SALVARRHYR FIHGIGRSGD ISAVQPKAAG SSLLNKITNS LVLDIIKLAG VHTVANCFVV PMATGMSLTL CFLTLRHKRP KAKYIIWPRI DQKSCFKSMI TAGFEPVVIE NVLEGDELRT DLKAVEAKVQ ELGPDCILCI HSTTSCFAPR VPDRLEELAV ICANYDIPHI VNNAYGVQSS KCMHLIQQGA RVGRIDAFVQ SLDKNFMVPV GGAIIAGFND SFIQEISKMY PGRASASPSL DVLITLLSLG SNGYKKLLKE RKEMFSYLSN QIKKLSEAYN ERLLHTPHNP ISLAMTLKTL DEHRDKAVTQ LGSMLFTRQV SGARVVPLGS MQTVSGYTFR GFMSHTNNYP CAYLNAASAI GMKMQDVDLF IKRLDRCLKA VRKERSKESD DNYDKTEDVD IEEMALKLDN VLLDTYQDAS S.
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 :
OTOR Human, HisDescription:
Otoraplin Human Recombinant, His Tag
Otoraplin, Melanoma Inhibitory Activity-Like Protein, Fibrocyte-Derived Protein, FDP, MIAL1, MIAL, Melanoma inhibitory activity-like protein.
Product # :
CYT-884Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
OTOR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (26-128 a.a) and having a molecular mass of 14.3kDa. OTOR is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OTOR protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness. -
Synonyms
Otoraplin, Melanoma Inhibitory Activity-Like Protein, Fibrocyte-Derived Protein, FDP, MIAL1, MIAL, Melanoma inhibitory activity-like protein.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMLASKK LCADDECVYT ISLASAQEDY NAPDCRFINV KKGQQIYVYS KLVKENGAGE FWAGSVYGDG QDEMGVVGYF PRNLVKEQRV YQEATKEVPT TDIDFFCE.
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 :
SERPINH1 HumanDescription:
Heat Shock 47kDa Human Recombinant
HSP47, HSP-47, Colligin-1, CBP1, Collagen Binding Protein-1, Serpin Peptidase Inhibitor Clade-H memebr 1, Serpin H1, Collagen-binding protein, Colligin, 47 kDa heat shock protein, Rheumatoid arthritis-related antigen RA-A47, Arsenic-transactivated protein 3, AsTP3, Cell proliferation-inducing gene 14 protein, SERPINH1, CBP2, gp46, PIG14, PPROM, RA-A47, SERPINH2.
Product # :
HSP-047Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human HSP47 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (18-418 a.a.) and having a molecular mass of 48.9 kDa. HSP47 human recombinant is fused to a 38 amino acid His Tag at N-terminus and purified by convential chromatogrpahy techniques.
Source
Escherichia Coli.
Formulation
The SERPINH1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SERPINH1 is part of the serpin superfamily of serine proteinase inhibitors. SEPINH1 expression is induced by heat shock. HSP47 localizes to the endoplasmic reticulum lumen and binds collagen therefore it is a molecular chaperone which takes part in the maturation of collagen molecules, facilitating the folding and assembly of procollagen molecules, retaining unfolded molecules within the ER, and assisting the transport of correctly folded-molecules from the ER to Golgi apparatus. Autoantibodies to HSP47 protein have been found in rheumatoid arthritis. SERPINH1 binds specifically to collagen and acts as a chaperone in the biosynthetic pathway of collagen.
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Synonyms
HSP47, HSP-47, Colligin-1, CBP1, Collagen Binding Protein-1, Serpin Peptidase Inhibitor Clade-H memebr 1, Serpin H1, Collagen-binding protein, Colligin, 47 kDa heat shock protein, Rheumatoid arthritis-related antigen RA-A47, Arsenic-transactivated protein 3, AsTP3, Cell proliferation-inducing gene 14 protein, SERPINH1, CBP2, gp46, PIG14, PPROM, RA-A47, SERPINH2.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAA EVKKPAAAAA PGTAEKLSPK AATLAERSAG LAFSLYQAMA KDQAVENILV SPVVVASSLG LVSLGGKATT ASQAKAVLSA EQLRDEEVHA GLGELLRSLS NSTARNVTWK LGSRLYGPSS VSFADDFVRS SKQHYNCEHS KINFRDKRSA LQSINEWAAQ TTDGKLPEVT KDVERTDGAL LVNAMFFKPH WDEKFHHKMV DNRGFMVTRS YTVGVMMMHR TGLYNYYDDE KEKLQIVEMP LAHKLSSLII LMPHHVEPLE RLEKLLTKEQ LKIWMGKMQK KAVAISLPKG VVEVTHDLQK HLAGLGLTEA IDKNKADLSR MSGKKDLYLA SVFHATAFEL DTDGNPFDQD IYGREELRSP KLFYADHPFI FLVRDTQSGS LLFIGRLVRP KGDKMRDEL.
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 :
CetrorelixDescription:
Cetrorelix
Product # :
HOR-277Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Cetrorelix acetate is a synthetic decapeptide with gonadotropin-releasing hormone (GnRH) antagonistic activity. Cetrorelix acetate is an analog of native GnRH with substitutions of amino acids at positions 1, 2, 3, 6, and 10. The molecular formula is C70H92CIN17O14 (Ac-D-Nal1-D-Cpa2-D-Pal3-Ser4-Tyr5- D-Cit6-Leu7-Arg8-Pro9-D -Ala10-NH2), and the molecular weight is 1431 Dalton, calculated as the anhydrous free base.
Formulation
The Cetrorelix 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
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cetrorelix although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cetrorelix 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.
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Solubility
It is recommended to reconstitute the lyophilized Cetrorelix 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.
- View Data Sheet
Name :
S100G HumanDescription:
S100 Calcium Binding Protein G Human Recombinant
Protein S100-G, Calbindin-D9k, S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, S100G, CABP9K, CALB3, S100D, CABP1, MGC138379.
Product # :
PRO-156Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
The Recombinant Human S100G produced in E.coli has a molecular mass of 10.04kDa containing 87 amino acid residues of the human S100G and fused to a 9 a.a. His tag at N-terminus.
Source
Escherichia Coli.
Formulation
S100G was filtered (0.4 µm) and lyophilized in 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.
More Info
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Introduction
S100G (calbindin D9K) is a vitamin D-dependent calcium-binding protein. S100G, which is a cytosolic protein, is a member of a family of calcium-binding proteins that includes calmodulin, parvalbumin, troponin C, and S100 protein. In the intestine, S100G is vitamin D-dependent and its expression correlates with calcium transport activity. S100G may increase Ca2+ absorption by buffering Ca2+ in the cytoplasm and increase ATP-dependent Ca2+ transport in duodenal basolateral membrane vesicles.
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Synonyms
Protein S100-G, Calbindin-D9k, S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, S100G, CABP9K, CALB3, S100D, CABP1, MGC138379.
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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.
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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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS TKKSPEELKRS TKKSPEELKR IFEKYAAKEG DPDQLSKDEL KLLIQAEFPS LLKGPNTLDD LFQELDKNGD GEVSFEEFQV LVKKISQ.
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Applications
Western blotting.
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 :
SDCBP2 HumanDescription:
Syndecan Binding Protein 2 Human Recombinant
SITAC, SITAC18, ST-2, Syntenin-2, Syndecan-binding protein 2.
Product # :
PRO-1297Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SDCBP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292 a.a.) and having a molecular mass of 34.0kDa. SDCBP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SDCBP2 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
SDCBP2 has two class II PDZ domains. PDZ domains assist protein-protein interactions by attaching to the cytoplasmic C-terminus of transmembrane proteins, and PDZ-containing proteins mediate cell signaling and the organization of protein complexes. SDCBP2 attaches to phosphatidylinositol 4, 5-bisphosphate (PIP2) and take part in nuclear PIP2 arrangement and cell division.
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Synonyms
SITAC, SITAC18, ST-2, Syntenin-2, Syndecan-binding protein 2.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSSLYPS LEDLKVDQAI QAQVRASPKM PALPVQATAI SPPPVLYPNL AELENYMGLS LSSQEVQESL LQIPEGDSTA VSGPGPGQMV APVTGYSLGV RRAEIKPGVR EIHLCKDERG KTGLRLRKVD QGLFVQLVQA NTPASLVGLR FGDQLLQIDG RDCAGWSSHK AHQVVKKASG DKIVVVVRDR PFQRTVTMHK DSMGHVGFVI KKGKIVSLVK GSSAARNGLL TNHYVCEVDG QNVIGLKDKK IMEILATAGN VVTLTIIPSV IYEHMVKKLP PVLLHHTMDH SIPDA.
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 :
SIGLEC9 HumanDescription:
Sialic Acid Binding Ig Like Lectin 9 Human Recombinant
Sialic Acid Binding Ig Like Lectin 9, Protein FOAP-9, Siglec-9, CDw329, Sialic Acid Binding Ig-Like Lectin 9, Sialic Acid-Binding Ig-Like Lectin 9, CD329 Antigen, OBBP-LIKE, FOAP-9, CD329.
Product # :
PRO-2447Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SIGLEC9 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 573 amino acids (18-348a.a.) and having a molecular mass of 63.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).SIGLEC9 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SIGLEC9 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Sialic Acid Binding Ig Like Lectin 9 (SIGLEC9) is a member of the sialic acid-binding Ig-like lectin family, which is a part of the immunoglobulin superfamily expressed mostly on human blood leukocytes. SIGLEC9 is a Putative adhesion molecule which is expressed in bone marrow, placenta, spleen, and fetal liver. SIGLEC9 is also a part of the recently characterized CD33-related Siglec family of sialic acid binding protein.
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Synonyms
Sialic Acid Binding Ig Like Lectin 9, Protein FOAP-9, Siglec-9, CDw329, Sialic Acid Binding Ig-Like Lectin 9, Sialic Acid-Binding Ig-Like Lectin 9, CD329 Antigen, OBBP-LIKE, FOAP-9, CD329.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADPQTSKLLT MQSSVTVQEG LCVHVPCSFS YPSHGWIYPG PVVHGYWFRE GANTDQDAPV ATNNPARAVW EETRDRFHLL GDPHTKNCTL SIRDARRSDA GRYFFRMEKG SIKWNYKHHR LSVNVTALTH RPNILIPGTL ESGCPQNLTC SVPWACEQGT PPMISWIGTS VSPLDPSTTR SSVLTLIPQP QDHGTSLTCQ VTFPGASVTT NKTVHLNVSY PPQNLTMTVF QGDGTVSTVL GNGSSLSLPE GQSLRLVCAV DAVDSNPPAR LSLSWRGLTL CPSQPSNPGV LELPWVHLRD AAEFTCRAQN PLGSQQVYLN VSLQSKATSG VTQGLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.
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.
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Name :
GLP-1 Human (31 a.a.)Description:
Glucagon Like Peptide-1 (31 a.a.) Human Recombinant
GLP1, GLP2, GRPP.
Product # :
HOR-236Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Glucagon Like Peptide-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 31 amino acids and having a molecular mass of 3.3 kDa. The GLP-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Recombinant GLP-1 concentrated solution (1mg/ml) was lyophilized after extensive dialyses against 0.1mg sodium phosphate monobasic & 1.6mg sodium phosphate dibasic.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Glucagon-like peptide-1 (GLP-1) is derived from the transcription product of the proglucagon gene. The major source of GLP-1 in the body is the intestinal L cell that secretes GLP-1 as a guthormone. The biologically active forms of GLP-1 are: GLP-1-(7-37) and GLP-1-(7-36)NH2.
GLP-1 secretion by L cells is dependent on the presence of nutrients in the lumen of the small intestine. The secretagogues (agents that causes or stimulates secretion) of this hormone include major nutrients like carbohydrate, proteinand lipid. Once in the circulation, GLP-1 has a half life of less than 2 minutes, due to rapid degradation by the enzyme dipeptidyl peptidase-4.
GLP-1 possesses several physiological properties that make it a subject of intensive investigation as a potential treatment of diabetes mellitus. The known physiological functions of GLP-1 include: Increases insulin secretion from the pancreas in a glucose-dependent manner, decreases glucagon secretion from the pancreas, increases beta cells mass and insulin gene expression, inhibits acid secretion and gastric emptying in the stomach, decreases food intake by increasing satiety. -
Synonyms
GLP1, GLP2, GRPP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Glucagon Like Peptide-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GLP-1 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.
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Solubility
It is recommended to reconstitute the lyophilized Glucagon Like Peptide-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HAEGTFTSDV SSYLEGQAAK EFIAWLVKGR G.
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.
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Name :
Tamm HorsfallDescription:
Recombinant Human Tamm Horsfall Glycoprotein
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
Product # :
ENZ-1206Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- SDS-PAGE
Description
Uromodulin Human Recombinant protein produced from HEK Cells, is a polypeptide chain containing 595 amino acids ( 25-613 a.a. ) and having a total Mw of 65 kDa.
Source
HEK293
Formulation
The UMOD protein was lyophilized from 0.4μm filtered solution containing 50mM NaCl, 0.02M TRIS, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE analysis.
SDS-PAGE
More Info
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Introduction
Uromodulin (Tamm–Horsfall protein) is produced mainly by cells in the kidney’s thick ascending limb and is the most abundant protein in normal urine.
Uromodulin takes part in salt and water regulation, helps prevent urinary tract infections and kidney stones, and influences inflammation and immune activity in the kidney.
Reduced Uromodulin levels is associated with chronic kidney disease.
UMOD mutations causes unproper protein folding and thus transported incorrectly, resulting in its accumulation inside kidney tubular cells that damages the tubules and cause kidney disease (ADTKD-UMOD), associated with high uric acid, gout, and progressive kidney failure.
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Synonyms
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized UMOD although stable at room temperature for 3 weeks, should be stored at -18C. Upon reconstitution UMOD should be stored at 4C between 2-7 days and for future use below -18C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
DTSEARWCSE CHSNATCTED EAVTTCTCQE GFTGDGLTCV DLDECAIPGA HNCSANSSCV NTPGSFSCVC PEGFRLSPGL GCTDVDECAE PGLSHCHALA TCVNVVGSYL CVCPAGYRGD GWHCECSPGS CGPGLDCVPE GDALVCADPC QAHRTLDEYW RSTEYGEGYA CDTDLRGWYR FVGQGGARMA ETCVPVLRCN TAAPMWLNGT HPSSDEGIVS RKACAHWSGH CCLWDASVQV KACAGGYYVY NLTAPPECHL AYCTDPSSVE GTCEECSIDE DCKSNNGRWH CQCKQDFNIT DISLLEHRLE CGANDMKVSL GKCQLKSLGF DKVFMYLSDS RCSGFNDRDN RDWVSVVTPA RDGPCGTVLT RNETHATYSN TLYLADEIII RDLNIKINFA CSYPLDMKVS LKTALQPMVS ALNIRVGGTG MFTVRMALFQ TPSYTQPYQG SSVTLSTEAF LYVGTMLDGG DLSRFALLMT NCYATPSSNA TDPLKYFIIQ DRCPHTRDST IQVVENGESS QGRFSVQMFR FAGNYDLVYL HCEVYLCDTM NEKCKPTCSG TRFRSGSVID QSRVLNLGPI TRKGVQATVH HHHHH
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Background
Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.
What is the molecular weight/Mw of UMOD Protein?
UMOD Protein has a total Mw of 65kDa.
What is the source or expression system of UMOD Protein?
HEK293.
What is the Purity of UMOD Protein?
UMOD Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of UMOD Protein?
The biological functionality of UMOD Protein will be determined in the future.
What is the amino acid sequence of UMOD Protein?
UMOD Protein is composed from 595 amino acids.
What applications can UMOD Protein be used in?
UMOD Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for UMOD Protein?
The endotoxin level is minimal, UMOD 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.