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1000 results found for “Prolactin PRL”
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Name :
GREM1 HumanDescription:
GREM1 Human Recombinant
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
Product # :
PRO-1359Price :
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Shipped with Ice Packs
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Description
GREM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (25-184) and having a molecular mass of 20.7 kDa. GREM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GREM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GREM1 belongs to the BMP (bone morphogenic protein) antagonist family. Like BMPs, BMP antagonists comprise cystine knots and usually form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, to which GREM1 belongs, is characterized by a C-terminal cystine knot with an eight-membered ring. The antagonistic effect of the secreted glycosylated protein is because of its direct binding to BMP proteins. As an antagonist of BMP, GREM1 takes a place in regulating organogenesis, body patterning, and tissue differentiation. In mouse, GREM1 has been shown to convey the sonic hedgehog (SHH) signal from the polarizing region to the apical ectodermal ridge during limb bud outgrowth. Alternatively merged transcript variants encoding different isoforms have been found for this gene.
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Synonyms
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
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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 MGSKKKGSQG AIPPPDKAQH NDSEQTQSPQ QPGSRNRGRG QGRGTAMPGE EVLESSQEAL HVTERKYLKR DWCKTQPLKQ TIHEEGCNSR TIINRFCYGQ CNSFYIPRHI RKEEGSFQSC SFCKPKKFTT MMVTLNCPEL QPPTKKKRVT RVKQCRCISI DLD.
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 :
CXCL2 HumanDescription:
GRO-Beta Human Recombinant (CXCL2)
Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.
Product # :
CHM-309Price :
Quantity :
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Shipped at Room temp
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Description
GRO-Beta Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7908 Dalton. The CXCL2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Chemokine (C-X-C motif) ligand 2 (CXCL2) is a small cytokine belonging to the CXC chemokine family that is also called macrophage inflammatory protein 2-alpha (MIP2-alpha), Growth-regulated protein beta (Gro-beta) and Gro oncogene-2 (Gro-2). CXCL2 is 90% identical in amino acid sequence as a related chemokine, CXCL1. This chemokine is secreted by monocytes and macrophages and is chemotactic for polymorphonuclear leukocytes and hematopoietic stem cells. The gene for CXCL2 is located on human chromosome 4 in a cluster of other CXC chemokines. CXCL2 mobilizes cells by interacting with a cell surface chemokine receptor called CXCR2.
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Synonyms
Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 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 GRO-beta Human 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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Leu-Ala-Thr.
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Background
What is the molecular weight/Mw of CXCL2 HUMAN Protein?
CXCL2 HUMAN Protein has a total Mw of 7.9kDa.
What is the source or expression system of CXCL2 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL2 HUMAN Protein?
CXCL2 HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL2 HUMAN Protein?
The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CXCL2 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Leu-Ala-Thr.
What applications can CXCL2 HUMAN Protein be used in?
CXCL2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL2 HUMAN Protein?
The endotoxin level is minimal, CXCL2 HUMAN 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 :
UPK2 HumanDescription:
Uroplakin 2 Human Recombinant
Uroplakin-2, UP2, Uroplakin II, UPII, UPK2.
Product # :
PRO-479Price :
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Shipped with Ice Packs
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Description
UPK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (26-155 a.a) and having a molecular mass of 16.2kDa.UPK2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UPK2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Uroplakin 2 (UPK2) is one of the proteins of the highly urothelium-specific integral membrane proteins of the asymmetric unit membrane which forms urothelium apical plaques in mammals. The asymmetric unit membrane is thought to strengthen the urothelium by preventing cell rupture during bladder distention. The UPK2 protein is expressed in the peripheral blood of bladder cancer patients with transitional cell carcinomas.
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Synonyms
Uroplakin-2, UP2, Uroplakin II, UPII, UPK2.
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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 MGSDFNISSL SGLLSPALTE SLLVALPPCH LTGGNATLMV RRANDSKVVT SSFVVPPCRG RRELVSVVDS GAGFTVTRLS AYQVTNLVPG TKFYISYLVK KGTATESSRE IPMSTLPRRN MESIGLGMAR TGG.
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 :
PURB HumanDescription:
Purine-Rich Element Binding Protein B Human Recombinant
Transcriptional activator protein Pur-beta, Purine-rich element-binding protein B, PURB, PURBETA.
Product # :
PRO-1969Price :
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Shipped with Ice Packs
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Description
PURB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-312) and having a molecular mass of 35.6 kDa.PURB is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PURB solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Purine-Rich Element Binding Protein B (PURB) is a single-stranded DNA-binding protein which takes part in the dendritic transport of a subset of mRNAs. PURB operates as repressor in myoblasts and fibroblasts in the control of vascular smooth muscle alpha-actin gene transcription. PURB binds preferentially to the single strand of the purine-rich element termed PUR, which is present at origins of replication and in gene flanking regions in various eukaryotes from yeasts through humans.
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Synonyms
Transcriptional activator protein Pur-beta, Purine-rich element-binding protein B, PURB, PURBETA.
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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 MGSMADGDSG SERGGGGGPC GFQPASRGGG EQETQELASK RLDIQNKRFY LDVKQNAKGR FLKIAEVGAG GSKSRLTLSM AVAAEFRDSL GDFIEHYAQL GPSSPEQLAA GAEEGGGPRR ALKSEFLVRE NRKYYLDLKE NQRGRFLRIR QTVNRGGGGF GAGPGPGGLQ SGQTIALPAQ GLIEFRDALA KLIDDYGGED DELAGGPGGG AGGPGGGLYG ELPEGTSITV DSKRFFFDVG CNKYGVFLRV SEVKPSYRNA ITVPFKAWGK FGGAFCRYAD EMKEIQERQR DKLYERRGGG SGGGEESEGE EVDED.
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 :
MAP1LC3A HumanDescription:
Microtubule-Associated Protein 1 Light Chain 3 Alpha Human Recombinant
ATG8E, LC3, LC3A, MAP1ALC3, MAP1BLC3, MLP3A.
Product # :
PRO-495Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MAP1LC3A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (1-120 a.a.) and having a molecular mass of 15.1 kDa. The MAP1LC3A is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAP1LC3A solution (1mg/ml) contains 20mM Tris-HCl pH-8.0, 1mM DTT, 0.1M NaCl & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
MAP1LC3A takes part in formation of autophagosomal vacuoles and is one of the light chain subunits that functions together with both MAP1A and/or MAP1B. MAP1LC3A has an important part in neuronal development and in maintaining the balance between neuronal plasticity and rigidity. MAP1LC3A is expressed as two alternatively spliced isoforms that are expressed in testis, brain, heart, liver and skeletal muscle, but are absent in thymus and peripheral blood leukocytes.
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Synonyms
ATG8E, LC3, LC3A, MAP1ALC3, MAP1BLC3, MLP3A.
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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
MPSDRPFKQR RSFADRCKEV QQIRDQHPSK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM SELVKIIRRR LQLNPTQAFF LLVNQHSMVS VSTPIADIYE QEKDEDGFLY MVYASQETFG LEHHHHHH.
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 :
HAPLN1 HumanDescription:
Hyaluronan And Proteoglycan Link Protein 1 Human Recombinant
Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.
Product # :
PRO-2012Price :
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Shipped with Ice Packs
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Description
HAPLN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (16-354 a.a.) and having a molecular mass of 40.9kDa.HAPLN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HAPLN1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Hyaluronan And Proteoglycan Link Protein 1, which is also known as HAPLN1 is a part of the HAPLN family.HAPLN1 contains one Ig-like V-type domain and two Link domains. In the extracellular cartilage matrix, HAPLN1 stabilizes the aggregates of proteoglycan monomers by means of hyaluronic acid .
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Synonyms
Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.
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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 MGSDHLSDNY TLDHDRAIHI QAENGPHLLV EAEQAKVFSH RGGNVTLPCK FYRDPTAFGS GIHKIRIKWT KLTSDYLKEV DVFVSMGYHK KTYGGYQGRV FLKGGSDSDA SLVITDLTLE DYGRYKCEVI EGLEDDTVVV ALDLQGVVFP YFPRLGRYNL NFHEAQQACL DQDAVIASFD QLYDAWRGGL DWCNAGWLSD GSVQYPITKP REPCGGQNTV PGVRNYGFWD KDKSRYDVFC FTSNFNGRFY YLIHPTKLTY DEAVQACLND GAQIAKVGQI FAAWKILGYD RCDAGWLADG SVRYPISRPR RRCSPTEAAV RFVGFPDKKH KLYGVYCFRA YN.
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 :
RASL12 HumanDescription:
RAS-Like Family 12 Human Recombinant
RAS-Like, Family 12, Ras Family Member Ris, Ras-Like Protein Ris, RIS, Ras-Like Protein Family Member 12, RASL12.
Product # :
PRO-2119Price :
Quantity :
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Shipped with Ice Packs
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Description
RASL12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 289 amino acids (1-266 a.a) and having a molecular mass of 32.1kDa.RASL12 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RASL12 protein solution (0.5mg/ml) containing 20mM Tirs-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
RAS-Like Family 12, also known as RASL12 belongs to the small GTPase superfamily, and to the Ras family.
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Synonyms
RAS-Like, Family 12, Ras Family Member Ris, Ras-Like Protein Ris, RIS, Ras-Like Protein Family Member 12, RASL12.
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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 MGSMSSVFGK PRAGSGPQSA PLEVNLAILG RRGAGKSALT VKFLTKRFIS EYDPNLEDTY SSEETVDHQP VHLRVMDTAD LDTPRNCERY LNWAHAFLVV YSVDSRQSFD SSSSYLELLA LHAKETQRSI PALLLGNKLD MAQYRQVTKA EGVALAGRFG CLFFEVSACL DFEHVQHVFH EAVREARREL EKSPLTRPLF ISEERALPHQ APLTARHGLA SCTFNTLSTI NLKEMPTVAQ AKLVTVKSSR AQSKRKAPTL TLLKGFKIF.
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 :
REG1B HumanDescription:
Regenerating Islet-Derived 1 Beta Human Recombinant
Lithostathine-1-beta, Regenerating protein I beta, REG1B, REGL.
Product # :
PRO-391Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human REG 1 beta manufactured with N-terminal fusion of His Tag. The Human REG 1 beta His-Tagged Fusion Protein, produced in E. coli, is 17.8 kDa protein containing 144 amino acid residues of the Human REG 1 beta and 12 additional amino acid residues – His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 20mM Tris, pH 8.0.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Reg protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system. -
Synonyms
Lithostathine-1-beta, Regenerating protein I beta, REG1B, REGL.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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 a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS HMQESQTELP NPRISCPEGT NAYRSYCYYF NEDPETWVDA DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SSTDDSNVWI GLHDPKKNRR WHWSSGSLVS YKSWDTGSPS SANAGYCASL TSCSGFKKWK DESCEKKFSF VCKFKN.
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 :
RELM b Human, HisDescription:
RELM-Beta Human Recombinant, His Tag
Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.
Product # :
CYT-454Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
RELM-beta Human Recombinant is a His-Tagged Fusion Protein which is 11 kDa protein containing 90 amino acid residues of the RELM-beta human and 12 additional amino acid residues - HisTag (underlined).
Source
Escherichia Coli.
Formulation
Filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
RELM-beta (Resistin-Like Molecule-beta) is a member of a recently identified family of secreted proteins containing a conserved cystein-rich C-terminus. The RELM family consists of resistin (also called FIZZ3), RELM-alfa (FIZZ1), RELM-beta (FIZZ2) and RELM-gamma. Only resisistin and RELM-beta were found in humans whereas all four RELM family members were identified in rodents.
RELM-beta appears to be produced as a homodimer exclusively by intestinal goblet cells and can be found in high quantities in stool. Remarkably, stool of germ-free mice displaying sterile intestinal tract does not contain RELM-beta until bacterial colonization takes place after pathogen-free mice entered natural environment. Some, but not all, colon carcinoma cell lines secrete RELM-beta into the cell culture supernatant.
The physiological function of RELM-beta is not known. High doses of recombinant RELM-beta showed hyperglycemic effects including lowered glucose disposal and increased hepatic glucose production in mice. -
Synonyms
Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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
Add 0.1M Acetate buffer pH-4 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.
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Amino Acid Sequence
MGSTQCSLDS VMDKKIKDVL NSLEYSPSPI SKKLSCASVK SQGRPSSCPA GMAVTGCACG YGCGSWDVQLETTCHCQCSV VDWTTARCCH LTKLRSHHHH HH.
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 :
RGS4 HumanDescription:
Regulator of G-Protein Signaling 4 Human Recombinant
Regulator of G-protein signaling 4, RGP4, RGS4, SCZD9.
Product # :
PRO-900Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RGS4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-205 a.a.) and having a molecular mass of 25.4kDa.RGS4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RGS4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Regulator of G protein signaling 4 (RGS4) is a protein which regulates G protein signaling. Regulator of G protein signaling (RGS) family members are regulatory molecules which act as GTPase activating proteins (GAPs) for G alpha subunits of heterotrimeric G proteins. Heterotrimeric G proteins serve to convey information from cell surface receptors to intracellular effectors.
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Synonyms
Regulator of G-protein signaling 4, RGP4, RGS4, SCZD9.
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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 MCKGLAGLPA SCLRSAKDMK HRLGFLLQKS DSCEHNSSHN KKDKVVICQR VSQEEVKKWA ESLENLISHE CGLAAFKAFL KSEYSEENID FWISCEEYKK IKSPSKLSPK AKKIYNEFIS VQATKEVNLD SCTREETSRN MLEPTITCFD EAQKKIFNLM EKDSYRRFLK SRFYLDLVNP SSCGAEKQKG AKSSADCASL VPQCA.
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 :
RPA2 HumanDescription:
Replication Protein A2 Human Recombinant
Replication protein A 32 kDa subunit, RP-A p32, Replication factor A protein 2, RF-A protein 2, Replication protein A 34 kDa subunit, RP-A p34, RPA2, REPA2, RPA32, RPA34.
Product # :
PRO-011Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RPA2 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 293 amino acids (1-270 a.a.) and having a molecular mass of 31.7kDa. The RPA2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RPA2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Replication Protein A2 (RPA2) is a single stranded DNA binding protein. Human RPA2 is a heterotrimeric protein containing subunits of 14, 32 and 70kDa. The RPA2 protein complex is highly conserved in eukaryotes and is crucial in DNA replication, homologous recombination and nucleotide excision repair. RPA2 C-terminus specifically interacts with the DNA repair enzyme UNG2 and repair factors XPA and Rad52, each of which functions in a different repair pathway. Additionally, RPA2 binds specifically to the SH2 domain of Stat3 in vivo, and overexpression of RPA2 corresponds to the augmented growth factor-stimulated tyrosine phosphorylation and transcription activities of Stat3.
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Synonyms
Replication protein A 32 kDa subunit, RP-A p32, Replication factor A protein 2, RF-A protein 2, Replication protein A 34 kDa subunit, RP-A p34, RPA2, REPA2, RPA32, RPA34.
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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 MGSMWNSGFE SYGSSSYGGA GGYTQSPGGF GSPAPSQAEK KSRARAQHIV PCTISQLLSA TLVDEVFRIG NVEISQVTIV GIIRHAEKAP TNIVYKIDDM TAAPMDVRQW VDTDDTSSEN TVVPPETYVK VAGHLRSFQN KKSLVAFKIM PLEDMNEFTT HILEVINAHM VLSKANSQPS AGRAPISNPG MSEAGNFGGN SFMPANGLTV AQNQVLNLIK ACPRPEGLNF QDLKNQLKHM SVSSIKQAVD FLSNEGHIYS TVDDDHFKST DAE.
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 :
Flt3 Ligand Human, HEKDescription:
Flt3-Ligand Human Recombinant, HEK derived
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Product # :
CYT-706Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Flt3-Ligand Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 24-30kDa due to glycosylation. The Flt3-Ligand is purified by proprietary chromatographic techniques.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
Flt3-Ligand was lyophilized from a 0.2µm filtered solution containing 1xPBS.
Purity
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
The activity was determined by the dose- dependent stimulation of the proliferation of the human acute myeloid leukemia cell line OCI-AML5. The ED50 is 0.56ng/ml.
More Info
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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
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Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-Ligand 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
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTAPQP.
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Background
What is the molecular weight/Mw of FLT3 LIGAND HUMAN, HEK Protein?
FLT3 LIGAND HUMAN, HEK Protein has a total Mw of 27kDa.
What is the source or expression system of FLT3 LIGAND HUMAN, HEK Protein?
HEK293 (Human Embryonic Kidney cell line).
What is the Purity of FLT3 LIGAND HUMAN, HEK Protein?
FLT3 LIGAND HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FLT3 LIGAND HUMAN, HEK Protein?
The activity was determined by the dose- dependent stimulation of the proliferation of the human acute myeloid leukemia cell line OCI-AML5. The ED50 is 0.56ng/ml.
What is the amino acid sequence of FLT3 LIGAND HUMAN, HEK Protein?
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTAPQP.
What applications can FLT3 LIGAND HUMAN, HEK Protein be used in?
FLT3 LIGAND HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FLT3 LIGAND HUMAN, HEK Protein?
The endotoxin level is minimal, FLT3 LIGAND HUMAN, HEK 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 :
LGALS3 Human, HisDescription:
Galectin-3 Human Recombinant, His Tag
Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.
Product # :
CYT-693Price :
Quantity :
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Shipped with Ice Packs
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- sds-page
Description
LGALS3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 270 amino acids (1-250 a.a.) and having a molecular mass of 28.3 kDa. The LGALS3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Galectin-3 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 for this effect is < 15ug/ml as measured by its ability to agglutinate human red blood cells.sds-page
More Info
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Introduction
Galectin-3 mediates with the alpha-3, beta-1 integrin the stimulation by cspg4 of endothelial cells migration. Galectin-3 plays an necessary part during the acquisition of vasculogenic mimicry and angiogenic properties associated with melanoma progression. LGALS3 overexpression is highly expressed in early stages of papillary carcinoma, and its expression intensity declines during tumor progression. Serum levels of LGALS3 are high in patients with thyroid malignancy but there is considerable overlap in serum LGALS3 concentrations between those with benign and malignant nodular thyroid disease. LGLAS3 takes part as an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.
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Synonyms
Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.
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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 MADNFSLHDA LSGSGNPNPQ GWPGAWGNQP AGAGGYPGAS YPGAYPGQAP PGAYPGQAPP GAYPGAPGAY PGAPAPGVYP GPPSGPGAYP SSGQPSATGA YPATGPYGAP AGPLIVPYNL PLPGGVVPRM LITILGTVKP NANRIALDFQ RGNDVAFHFN PRFNENNRRV IVCNTKLDNN WGREERQSVF PFESGKPFKI QVLVEPDHFK VAVNDAHLLQ YNHRVKKLNE ISKLGISGDI DLTSASYTMI.
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Background
What is the molecular weight/Mw of LGALS3 HUMAN, HIS Protein?
LGALS3 HUMAN, HIS Protein has a total Mw of 28.3kDa.
What is the source or expression system of LGALS3 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of LGALS3 HUMAN, HIS Protein?
LGALS3 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS3 HUMAN, HIS Protein?
The ED50 for this effect is < 2.5ug/ml as measured by its ability to agglutinate human red blood cells.
What is the amino acid sequence of LGALS3 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MADNFSLHDA LSGSGNPNPQ GWPGAWGNQP AGAGGYPGAS YPGAYPGQAP PGAYPGQAPP GAYPGAPGAY PGAPAPGVYP GPPSGPGAYP SSGQPSATGA YPATGPYGAP AGPLIVPYNL PLPGGVVPRM LITILGTVKP NANRIALDFQ RGNDVAFHFN PRFNENNRRV IVCNTKLDNN WGREERQSVF PFESGKPFKI QVLVEPDHFK VAVNDAHLLQ YNHRVKKLNE ISKLGISGDI DLTSASYTMI.
What applications can LGALS3 HUMAN, HIS Protein be used in?
LGALS3 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS3 HUMAN, HIS Protein?
The endotoxin level is minimal, LGALS3 HUMAN, HIS 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 :
PRPS1 HumanDescription:
Phosphoribosyl Pyrophosphate Synthetase 1 Human Recombinant
ARTS, CMTX5, PPRibP, PRSI, DFN2, Ribose-phosphate pyrophosphokinase 1, DFNX1, Phosphoribosyl pyrophosphate synthase I, PRS-I, PRPS1, KIAA0967.
Product # :
PKA-361Price :
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Description
PRPS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 338 amino acids (1-318 a.a.) and having a molecular weight of 36.9kDa.The PRPS1 is fused to 20 a.a His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PRPS1 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
PRPS1 catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. PRPS1 catalyzes the phosphoribosylation of ribose 5-phosphate to 5-phosphoribosyl-1-pyrophosphate, which is essential for purine metabolism and nucleotide biosynthesis. Defects in PRPS1 result in phosphoribosylpyrophosphate synthetase superactivity, Charcot-Marie-Tooth disease X-linked recessive type 5 and Arts Syndrome.
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Synonyms
ARTS, CMTX5, PPRibP, PRSI, DFN2, Ribose-phosphate pyrophosphokinase 1, DFNX1, Phosphoribosyl pyrophosphate synthase I, PRS-I, PRPS1, KIAA0967.
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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 MPNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIGESVRG EDVYIVQSGC GEINDNLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK DKSRAPISAK LVANMLSVAG ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLKWIRENIS EWRNCTIVSP DAGGAKRVTS IADRLNVDFA LIHKERKKAN EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG ATRVYAILTH GIFSGPAISR INNACFEAVV VTNTIPQEDK MKHCSKIQVI DISMILAEAI RRTHNGESVS YLFSHVPL.
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 :
Protein-L CysDescription:
Protein L Cys Recombinant
Product # :
PRO-1931Price :
Quantity :
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Shipped at Room temp
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- sds-page, HPLC
Description
Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 366 amino acids in total and having a molecular mass of 40.6kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-L was lyophilized without any additives.
Purity
Greater than 96.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.sds-page, HPLC
More Info
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Introduction
The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L 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 Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAGC.
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 :
Super Leptin qA OvineDescription:
Super Leptin Antagonist Ovine Recombinant
Product # :
CYT-1245Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Super Leptin Antagonist Ovine Recombinant is a single polypeptide chain containing 146 amino acids, an additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa. Super Ovine Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
ProSpec’s super Ovine leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Super Ovine leptin antagonist also inhibits various leptin effects in several in vitro bioassays.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super Ovine leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super Ovine leptin antagonist 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.
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Solubility
It is recommended to reconstitute the lyophilized Super Leptin Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 10, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
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Background
Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviours which save energy. When leptin levels are high, the brain interprets 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.
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Protein content
Protein quantitation 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 :
Leptin Receptor ChickenDescription:
Leptin Receptor Chicken Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.
Product # :
CYT-509Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Leptin Binding Domain Chicken Recombinant also called Leptin Receptor produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 208 amino acids and having a molecular mass of 24.5 kDa. Chicken Leptin Receptor consists of the cytokine binding domain of leptin receptor amino acids 420-626 of chicken leptin receptor.The Leptin Binding Domain is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was filter sterilized and stored at 4°C (0.2 to 0.5 mg/ml) solution of Tris-HCl buffer, pH 9.0 with 150mM NaCl.
Purity
Greater than 99.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Leptin Receptor is a part of the gp130 family of cytokine receptors that stimulate gene transcription by activating cytosolic STAT proteins. Leptin Receptor plays a role in the regulation of fat metabolism and in novel hematopoietic pathway that is obligatory for normal lymphopoiesis. Leptin Receptorparticipates in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus.Leptin Receptoraffectsspecifically on T lymphocyte responses.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.
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Physical Appearance
Sterile Filtered colorless solution at a concentration of 0.4 mg/ml.
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Stability
Sterile solutions at 0.5mg/ml or less are stable at 4°C for several months.
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Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Ile-Asp-Val-Asn-Ile Biological ActivityBiological Activity is evidenced by high affinity binding of mammalian leptins at 1:1 molar ratio.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 2.45 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 Leptin Binding Domain 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 :
IGF1 HumanDescription:
IGF-1 Human Recombinant
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.
Product # :
CYT-216Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IGF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.6kDa.IGF-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated solution in PBS, pH 7.0.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity was determined by the cell proliferation assay using serum free human MCF-7 cells in <2ng/ml, corresponding to a Specific Activity of >5.0 x 105IU/mg.
More Info
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Introduction
The somatomedins, IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B.
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Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 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 IGF-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
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
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Background
IGF stands for INS like growth factors, which are proteins that have a high similarity to INS. They are part of a complicated process that uses cells to communication with the physiologic environment around them. IGF’s complex system is often called the ‘axis’. This consists of:
● Two cell-surface receptors (IGF1R and IGF2R)
● Two ligands (IGF-1 and IGF-2)
● A family of six high-affinity IGF-binding proteins.
● Proteases.The Effect IGF Has On The Body
Many unique tissue types express the IGF-1 receptor, and the effects can vary. It induces the survival of neurons, may catalyse skeletal muscle hypertrophy by inducing protein synthesis, and by blocking muscle atrophy. It works as a protector for cartilage cells, and may work to be an anabolic factor for the bones. When used in high concentrations, it can activate the INS receptor, and can even complement the effects that INS has on the body.Diseases And IGF
Diseases and IGF are closely related, and a number of them can be affected. The INS IGF axis is thought to have an effect on aging, with an increased life span shown in fruit flies when used in studies.
It is also important to note the crucial role that IGF plays in cancer and diabetes - IGF- 1 has been shown to stimulate growth in both prostate and breast cancer cells. The degree of risk that IGF-1 poses is up for debate, and many scientists are not in agreement. IGF has also shown to have the ability to decrease blood glucose levels, although not quite as effective as INS.How Was IGF Discovered?
Investigators began studying the effects of biological substances on cells and tissues outside the body when IGFs were discovered. The name is self explanatory in the fact that IGF performs INS actions in some tissues, but is less potent than INS at decreasing blood sugar. Its fundamental action is to stimulate growth, whether that be within the epidermal growth factor or the nerve growth factor.What’s The Difference Between IGF-1 And IGF-2?
The two types of IGF are IGF-1 and IGF-2. Although the names are similar, the specific actions that they take are different - they bind and activate completely difference receptors. The major actor in them both is the effect that they have on cell growth. Most of the actions of the pituitary GH are mediated by IGFs, but predominantly IGF-1. GH works to stimulate many tissues within the body, especially the liver which then secretes IGF-1. This then causes hypertrophy, or in layman's terms, an increase in cell size, as well as hyperplasia which is an increase in the number of cells.
The IGF-1 concentration will increase during childhood and hit peak during puberty, but will then decrease afterwards, as does the hormone secretion itself. It has been proven that children and adults with a deficiency of the GH have low serum IGF-1 concentrations when put in comparison with others in the same age range. Patients who have conditions like acromegaly have been shown to have increased serum IGF-1 concentrations. The production of IGF-2 is less dependent on the secretion of GH than IGF-1, and is much less important for stimulating linear growth.
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 :
LAYN HumanDescription:
Layilin Human Recombinant
Layilin
Product # :
PRO-1629Price :
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Shipped with Ice Packs
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Description
LAYN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (22-235) and having a molecular mass of 26.7kDa.LAYN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LAYN solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
LAYN, also known as Layilin, contains 1 c-type lectin domain. This protein is receptor for hyaluronate and Interacts with NF2, RDX and TLN1. The C-terminal domain interacts with the N-terminal domain of RDX.
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Synonyms
Layilin
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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 MGSATGRLLS ASDLDLRGGQ PVCRGGTQRP CYKVIYFHDT SRRLNFEEAK EACRRDGGQL VSIESEDEQK LIEKFIENLL PSDGDFWIGL RRREEKQSNS TACQDLYAWT DGSISQFRNW YVDEPSCGSE VCVVMYHQPS APAGIGGPYM FQWNDDRCNM KNNFICKYSD EKPAVPSREA EGEETELTTP VLPEETQEED AKKTFKESRE AALNLAY
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 :
PNPO AntibodyDescription:
Pyridoxamine 5'-Phosphate Oxidase, Mouse Anti Human
Pyridoxine-5'-phosphate oxidase, Pyridoxamine-phosphate oxidase, PNPO, PDXPO, FLJ10535.
Product # :
ANT-063Price :
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
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Introduction
Pyridoxine-5'-phosphate oxidase (PNPO) is the rate-limiting enzyme in vitamin B6 synthesis. Vitamin B6 (Pyridoxal 5-prime-phosphate or PLP) is vital for normal cellular function, and some cancer cells have notable differences in vitamin B6 metabolism compared to their normal counterparts.Vitamin B6 is an essential co-factor for enzymes involved in both homocysteine metabolism and synthesis of neurotransmitters such as catecholamine. Mutations in the PNPO gene result in PNPO deficiency, a form of neonatal epileptic encephalopathy.
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Synonyms
Pyridoxine-5'-phosphate oxidase, Pyridoxamine-phosphate oxidase, PNPO, PDXPO, FLJ10535.
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Immunogen
Anti-human PNPO mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PNPO amino acids 57-261 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
PAT2C7AT.
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Applications
PNPO antibody has been tested by ELISA and 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 ~ 1:5000.
Recommended starting dilution is 1:1000. -
Type
Mouse Anti Human Monoclonal.
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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.
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Purification Method
PNPO 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 :
VHL PAT82B10AT AntibodyDescription:
Von Hippel-Lindau Protein, Clone PAT82B10AT, Mouse Anti Human
Von Hippel-Lindau disease tumor suppressor, pVHL, Protein G7, VHL, RCA1, VHL1, HRCA1.
Product # :
ANT-722Price :
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
Von Hippel-Lindau disease is a dominant inherited syndrome characterized by the predisposition to develop various kinds of benign and malignant tumors, including clear cell renal carcinomas, pheochromocytomas and hemangioblastomas of the central nervous system and retina. VHL syndrome is caused by germline mutation in the VHL tumor suppressor, and VHL tumors are associated with loss or mutation of the remaining wild-type allele. VHL has two domains: a roughly 100-residue NH2-terminal domain rich in b sheet (b-domain) and a smaller a-helical domain (a-domain), held together by two linkers and a polar interface. VHL protein is also involved in the degradation of hypoxia-inducible factor (HIF).
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Synonyms
Von Hippel-Lindau disease tumor suppressor, pVHL, Protein G7, VHL, RCA1, VHL1, HRCA1.
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Immunogen
Anti-human VHL mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human VHL protein 1-154 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and k light chain.
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Clone
PAT82B10AT.
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Applications
VHL antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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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.
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Purification Method
VHL 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 :
IFNG MouseDescription:
IFN-Gamma Mouse Recombinant
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
Product # :
CYT-358Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IFN-gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids and having a molecular mass of 15.6kDa.The IFN-gamma is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4 and 5% trehalose.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg
More Info
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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs. -
Synonyms
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IFN-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma 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 IFN-gamma in sterile distilled water or 20mM AcOH at concentrations ranging between 0.1mg-0.5mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.
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Background
What is the molecular weight/Mw of IFNG MOUSE Protein?
IFNG MOUSE Protein has a total Mw of 15.6kDa.
What is the source or expression system of IFNG MOUSE Protein?
Escherichia Coli.
What is the Purity of IFNG MOUSE Protein?
IFNG MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG MOUSE Protein?
The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg
What is the amino acid sequence of IFNG MOUSE Protein?
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.
What applications can IFNG MOUSE Protein be used in?
IFNG MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG MOUSE Protein?
The endotoxin level is minimal, IFNG 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 :
PKAkt1/PKBa HumanDescription:
Protein Kinase Akt1/PKB alpha, Inactive enzyme Human Recombinant
RAC-alpha serine/threonine-protein kinase, EC 2.7.11.1, RAC-PK-alpha, Protein kinase B, PKB, C-AKT, AKT1, AKT, RAC, PRKBA, MGC99656, RAC-ALPHA.
Product # :
PKA-207Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
PKAkt1 is a glycosilated polypeptide having a molecular mass of 59.1 kDa, fused with a polyhistidine tag at N-terminus (to facilitate removal of Akt1 kinase from the reaction mixture).Inactive enzyme, suitable for negative control experiments or for phosphorylation as a substrate.Recombinant Protein Kinase B is purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
PKAkt1 in 50mM Tris-HCl, 100mM NaCl, 1mM DTT, 25mM beta glycerophosphate, 50% glycerol, pH 8.5.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
No protease activity (Twinning test).
The Specific activity is 235 U/mg.More Info
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Introduction
Akt1, also known as "Akt" or protein kinaseB (PKB) is an important molecule in mammaliancellular signaling.
In humans, there are three genes in the "Akt family": Akt1, Akt2, and Akt3. These enzymesare members of the serine/threonine-specific protein kinasefamily (EC2.7.11.1).
Akt1 is involved in cellular survival pathways, by inhibiting apoptoticprocesses. Akt1 is also able to induce protein synthesispathways, and is therefore a key signaling protein in the cellular pathways that lead to skeletal muscle hypertrophy, and general tissue growth. Since it can block apoptosis, and thereby promote cell survival, Akt1 has been implicated as a major factor in many types of cancer. Akt (now also called Akt1) was originally identified as the oncogenein the transforming retrovirus, AKT8. -
Synonyms
RAC-alpha serine/threonine-protein kinase, EC 2.7.11.1, RAC-PK-alpha, Protein kinase B, PKB, C-AKT, AKT1, AKT, RAC, PRKBA, MGC99656, RAC-ALPHA.
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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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Unit Definition
1 Unit is defined as 1 picomole phosphate transferred to the synthetic peptide (RPRAATF) per min at 30°C.
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 :
Thrombopoietin HumanDescription:
Thrombopoietin Human Recombinant
Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO
Product # :
CYT-1178Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
TPO Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain containing 343 amino acids (22-353 a.a) and having a molecular mass of 36.8kDa.TPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
TPO protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range is ≤10ng/ml. It is measured by cell proliferation assay using MO7e human megakaryocytic leukemic cells.
More Info
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Introduction
Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidney which regulates the production of platelets by the bone marrow. TPO stimulates the production as well as differentiation of megakaryocytes, the bone marrow cells which fragment into large numbers of platelets.
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Synonyms
Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO
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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
DGSHMSPAPP ACDLRVLSKL LRDSHVLHSR LSQCPEVHPL PTPVLLPAVD FSLGEWKTQM EETKAQDILG AVTLLLEGVM AARGQLGPTC LSSLLGQLSG QVRLLLGALQ SLLGTQLPPQ GRTTAHKDPN AIFLSFQHLL RGKVRFLMLV GGSTLCVRRA PPTTAVPSRT SLVLTLNELP NRTSGLLETN FTASARTTGS GLLKWQQGFR AKIPGLLNQT SRSLDQIPGY LNRIHELLNG TRGLFPGPSR RTLGAPDISS GTSDTGSLPP NLQPGYSPSP THPPTGQYTL FPLPPTLPTP VVQLHPLLPD PSAPTPTPTS PLLNTSYTHS QNLSQEGHHH 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.