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1000 results found for “Karyopherin”
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Name :
TPM4 HumanDescription:
Tropomyosin-4 Human Recombinant
Tropomyosin alpha-4 chain, TM30p1, Tropomyosin-4, TPM4.
Product # :
PRO-187Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TPM4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 268 amino acids (1-248 a.a.) and having a molecular mass of 30.7kDa.TPM4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TPM4 solution (1 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
TPM4 is a member of the tropomyosin family. Tropomyosins exist in practically all eukaryotic cells (both muscle and nonmuscle), where they bind actin filaments and function to modulate actin-myosin interaction and stabilize actin filament structure. TPM4 binds to actin filaments in muscle and nonmuscle cells and plays a central role, in connection with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction.
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Synonyms
Tropomyosin alpha-4 chain, TM30p1, Tropomyosin-4, TPM4.
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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 MAGLNSLEAV KRKIQALQQQ ADEAEDRAQG LQRELDGERE RREKAEGDVA ALNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK DEEKMEIQEM QLKEAKHIAE EADRKYEEVA RKLVILEGEL ERAEERAEVS ELKCGDLEEE LKNVTNNLKS LEAASEKYSE KEDKYEEEIK LLSDKLKEAE TRAEFAERTV AKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ TLNELNCI.
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 :
FGF4 HumanDescription:
Fibroblast Growth Factor-4 Human Recombinant
HBGF4, FGF-4, FGF4, KFGF, HSTF1.
Product # :
CYT-312Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
FGF4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids and having a molecular mass of 19.8kDa. The FGF4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FGF4 protein was lyophilized with 20mM sodium phosphate and 500mM NaCl pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X106 units/mg.
More Info
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Introduction
FGF4 holds s comprehensive mitogenic and cell survival activities and takes part in a range of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF4 possess oncogenic transforming activity. FGF4 and FGF3, oncogenic growth factors are localized on chromosome 11. Co-amplification of both factors was found in several kinds of human tumors. FGF4 functions in bone morphogenesis and limb development through the sonic hedgehog (SHH) signaling pathway.
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Synonyms
HBGF4, FGF-4, FGF4, KFGF, HSTF1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized FGF4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-4 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 FGF4 Human Recombinant 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
MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.
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Background
What is the molecular weight/Mw of FGF4 HUMAN Protein?
FGF4 HUMAN Protein has a total Mw of 19.8kDa.
What is the source or expression system of FGF4 HUMAN Protein?
Escherichia Coli.
What is the Purity of FGF4 HUMAN Protein?
FGF4 HUMAN Protein is > 95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF4 HUMAN Protein?
The ED50 as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X106 units/mg.
What is the amino acid sequence of FGF4 HUMAN Protein?
MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.
What applications can FGF4 HUMAN Protein be used in?
FGF4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF4 HUMAN Protein?
The endotoxin level is minimal, FGF4 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 :
GDF10 HumanDescription:
Growth differentiation factor 10 Human Recombinant
Bone morphogenetic protein 3b, BMP-3b, Growth/differentiation factor 10, GDF-10, Bone-inducing protein, BIP, GDF10, BMP3B.
Product # :
CYT-659Price :
Quantity :
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Shipped with Ice Packs
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- sds-page
Description
GDF10 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids (369-478 a.a.) and having a total molecular mass of 12.5 kDa. GDF10 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GDF10 solution (1mg/ml) contains 10mM Sodium citrate (pH 3.5), 1mM DTT, 40% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
GDF10 is a member of the BMP family and the TGF-beta superfamily. GDF10 is expressed in femur, brain, lung, skeletal, muscle, pancreas and testis, and has a role in head formation and possibly multiple roles in skeletal morphogenesis. In humans, GDF10 mRNA is found in the cochlea and lung of fetuses, and in testis, retina, pineal gland, and other neural tissues of adults. The BMP family members are regulators of cell growth and differentiation in both embryonic and adult tissues. These proteins are characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing 7 conserved cysteine residues.
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Synonyms
Bone morphogenetic protein 3b, BMP-3b, Growth/differentiation factor 10, GDF-10, Bone-inducing protein, BIP, GDF10, BMP3B.
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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
MQWDEPRVCS RRYLKVDFAD IGWNEWIISP KSFDAYYCAG ACEFPMPKIV RPSNHATIQS IVRAVGIIPG IPEPCCVPDK MNSLGVLFLD ENRNVVLKVY PNMSVDTCAC R.
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Background
What is the molecular weight/Mw of GDF10 HUMAN Protein?
GDF10 HUMAN Protein has a total Mw of 12.5kDa.
What is the source or expression system of GDF10 HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF10 HUMAN Protein?
GDF10 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF10 HUMAN Protein?
The biological functionality of GDF10 HUMAN Protein will be determined in the future.
What is the amino acid sequence of GDF10 HUMAN Protein?
MQWDEPRVCS RRYLKVDFAD IGWNEWIISP KSFDAYYCAG ACEFPMPKIV RPSNHATIQS IVRAVGIIPG IPEPCCVPDK MNSLGVLFLD ENRNVVLKVY PNMSVDTCAC R.
What applications can GDF10 HUMAN Protein be used in?
GDF10 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF10 HUMAN Protein?
The endotoxin level is minimal, GDF10 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 :
PTH (7-84) N15 HumanDescription:
Parathyroid Hormone (7-84) N15 Labeled Human Recombinant
Parathyrin, PTH, Parathormone.
Product # :
HOR-013Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PTH (7-84) N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 8900 Dalton labeled by the stable isotope N15.The PTH (7-84) N15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PTH (7-84) N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calcium in the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptor in three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone. In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb. In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylation of 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
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Synonyms
Parathyrin, PTH, Parathormone.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PTH (7-84) N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PTH (7-84) N15 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 PTH (7-84) N15 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
LMHNLGKHLN SMERVEWLRK KLQDVHNFVA LGAPLAPRDA GSQRPRKKED NVLVESHEKS LGEADKADVN VLTKAKSQ
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 :
MRPL28 HumanDescription:
Mitochondrial Ribosomal Protein L28 Human Recombinant
MAAT1, p15, 39S ribosomal protein L28, mitochondrial, L28mt, MRP-L28, Melanoma-associated antigen recognized by T-lymphocytes.
Product # :
PRO-1279Price :
Quantity :
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Shipped with Ice Packs
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Description
MRPL28 Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (56-256) and having a molecular mass of 25.8 kDa. MRPL28 is fused to 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MRPL28 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.5), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
MRPL28 is found in a variety of normal tissues such as spleen, testis, thymus, liver, kidney, brain, adrenal, lung and retinal tissue. 39S ribosomal protein L28, mitochondrial (MRPL28), is a part of the ribosomal protein L28P family. Mammalian mitochondrial ribosomal proteins encoded by nuclear genes and helps in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPL28 is an important therapeutic reagent for HLA-A24 (A24) patients since this antigen is distinguished by tumor-infiltrating lymphocyte (TIL) 1290, which targets the A24 serotype.
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Synonyms
MAAT1, p15, 39S ribosomal protein L28, mitochondrial, L28mt, MRP-L28, Melanoma-associated antigen recognized by T-lymphocytes.
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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 MNGQRERVED VPIPIYFPPE SQRGLWGGEG WILGQIYANN DKLSKRLKKV WKPQLFEREF YSEILDKKFT VTVTMRTLDL IDEAYGLDFY ILKTPKEDLC SKFGMDLKRG MLLRLARQDP QLHPEDPERR AAIYDKYKEF AIPEEEAEWV GLTLEEAIEK QRLLEEKDPV PLFKIYVAEL IQQLQQQALS EPAVVQKRAS GQ.
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 :
E Selectin HumanDescription:
E-selectin Human Recombinant
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-380Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
E-Selectin Human Recombinant is expressed in E. coli containing amino acids 179-557 fused to an amino terminal hexahistidine tag, having a total molecular weight of 45.22 kDa.
Source
Escherichia Coli.
Formulation
E-Selectin is supplied in 1x PBS and 50% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.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 liquid formulation.
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Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NME3 Human, ActiveDescription:
Non-Metastatic Cells 3 Human Recombinant, BioActive
Nucleoside diphosphate kinase 3, c371H6.2, DR-nm23, KIAA0516, NDPK-C, NDPKC, NM23-H3, NM23H3.
Product # :
PRO-2641Price :
Quantity :
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Shipped with Ice Packs
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Description
NME3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (22-169 a.a.) and having a molecular mass of 19.1kDa.NME3 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NME3 solution (0.5mg/ml) contains 50% glycerol, 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 150unit/mg, and is defined as the amount of enzyme that convert 1.0 umole each of ATP and TDP to ADP and TTP per minute at pH 7.5 at 25C in a couple system with PK/LDH.
More Info
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Introduction
Non-Metastatic Cells 3 or NME3 is a possible suppressor of metastasis. NME3 can be found at a lower levels in greatly metastatic cells when compared to cells that has less metastatic potential NME3 is crucial for the nucleoside triphosphates synthesis, also, in apoptosis induction & hematopoiesis. NME3 is can be expressed during early stages of myeloid differentiation of greatly purified CD34+ cells.
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Synonyms
Nucleoside diphosphate kinase 3, c371H6.2, DR-nm23, KIAA0516, NDPK-C, NDPKC, NM23-H3, NM23H3.
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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 MERTFLAVKP DGVQRRLVGE IVRRFERKGF KLVALKLVQA SEELLREHYA ELRERPFYGR LVKYMASGPV VAMVWQGLDV VRTSRALIGA TNPADAPPGT IRGDFCIEVG KNLIHGSDSV ESARREIALW FRADELLCWE DSAGHWLYE
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 :
ATP5H HumanDescription:
ATP Synthase Mitochondrial Fo Complex Subunit D Human Recombinant
ATP Synthase H+ Transporting, Mitochondrial Fo Complex Subunit D, ATP Synthase D Chain Mitochondrial, ATP Synthase H+ Transporting Mitochondrial F1F0 Subunit D, ATPase Subunit D, My032 Protein, ATPQ.
Product # :
PRO-1631Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ATP5H Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (1-161) and having a molecular mass of 20.9kDa.ATP5H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ATP5H solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
ATP5H is a member of the ATPase d subunit family and encodes the d subunit of the F0 complex. Electron transport complexes of the respiratory chain create a proton gradient across the membrane which induces ATP5H to transform ADP to ATP. Two alternatively spliced isoforms of ATP5H, encoded by a gene that maps to human chromosome 17q25.1, are known. ATP5H is restricted to mitochondrial inner membrane.
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Synonyms
ATP Synthase H+ Transporting, Mitochondrial Fo Complex Subunit D, ATP Synthase D Chain Mitochondrial, ATP Synthase H+ Transporting Mitochondrial F1F0 Subunit D, ATPase Subunit D, My032 Protein, ATPQ.
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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 MGSMAGRKLA LKTIDWVAFA EIIPQNQKAI ASSLKSWNET LTSRLAALPE NPPAIDWAYY KANVAKAGLV DDFEKKFNAL KVPVPEDKYT AQVDAEEKED VKSCAEWVSL SKARIVEYEK EMEKMKNLIP FDQMTIEDLN EAFPETKLDK KKYPYWPHQP IENL
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 :
PAX8 HumanDescription:
Paired Box 8 Human Recombinant
Paired Box 8, Paired Box Gene 8, PAX8.
Product # :
PRO-2134Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PAX8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-287 a.a) and having a molecular mass of 33.4kDa.PAX8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PAX8 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Paired box 8, also known as PAX8 functions in thyroid follicular cell development as well as in expression of thyroid-specific genes. PAX8 complexes with TTF-1& TTF-2 in order to stimulate thyroid follicular cell differentiation and thyroid hormone biosynthesis by regulating the expression of NIS (sodium iodide symporter) , TPO (thyroid peroxidase), TG (thyroglobulin) and the TSHR (thyrotropin receptor). Defects in PAX8 are the cause of CHNG2 (congenital hypothyroidism non-goitrous type 2).
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Synonyms
Paired Box 8, Paired Box Gene 8, PAX8.
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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 MGSMPHNSIR SGHGGLNQLG GAFVNGRPLP EVVRQRIVDL AHQGVRPCDI SRQLRVSHGC VSKILGRYYE TGSIRPGVIG GSKPKVATPK VVEKIGDYKR QNPTMFAWEI RDRLLAEGVC DNDTVPSVSS INRIIRTKVQ QPFNLPMDSC VATKSLSPGH TLIPSSAVTP PESPQSDSLG STYSINGLLG IAQPGSDKRK MDDSDQDSCR LSIDSQSSSS GPRKHLRTDA FSQHHLEPLE CPFERQHYPE AYASPSHTKG EQEVNTLAMP MATPPTPPTA RPGASPTPAC
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 :
PPIL4 HumanDescription:
Peptidylprolyl Isomerase (Cyclophilin)-Like 4 Human Recombinant
Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.
Product # :
ENZ-026Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PPIL4 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 512 amino acids (1-492 a.a.) and having a molecular mass of 59.3kDa. The PPIL4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PPIL 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.
Biological Activity
Specific activity is > 190 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.More Info
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Introduction
PPIL4 belongs to an evolutionarily conserved cyclophilin-type PPIase family of proteins. PPIL4, which is ubiquitously expressed with predominant expression in kidney localizes to the nucleus and contains one PPIase cyclophilin-type domain, a lysine-rich domain, a pair of bipartite nuclear targeting sequences and one RRM (RNA recognition motif) domain. The presence of the RRM domain along with nuclear targeting sequences implies that PPIL4 may be involved in transcriptional regulation.
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Synonyms
Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.
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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 MAVLLETTLG DVVIDLYTEE RPRACLNFLK LCKIKYYNYC LIHNVQRDFI IQTGDPTGTG RGGESIFGQL YGDQASFFEA EKVPRIKHKK KGTVSMVNNG SDQHGSQFLI TTGENLDYLD GVHTVFGEVT EGMDIIKKIN ETFVDKDFVP YQDIRINHTV ILDDPFDDPP DLLIPDRSPE PTREQLDSGR IGADEEIDDF KGRSAEEVEE IKAEKEAKTQ AILLEMVGDL PDADIKPPEN VLFVCKLNPV TTDEDLEIIF SRFGPIRSCE VIRDWKTGES LCYAFIEFEK EEDCEKAFFK MDNVLIDDRR IHVDFSQSVA KVKWKGKGGK YTKSDFKEYE KEQDKPPNLV LKDKVKPKQD TKYDLILDEQ AEDSKSSHSH TSKKHKKKTH HCSEEKEDED YMPIKNTNQD IYREMGFGHY EEEESCWEKQ KSEKRDRTQN RSRSRSRERD GHYSNSHKSK YQTDLYERER SKKRDRSRSP KKSKDKEKSK YR.
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 :
CDHR5 MouseDescription:
Cadherin Related Family Member 5 Mouse Recombinant
Cadherin-related family member 5, Mu-protocadherin, Cdhr5, Mucdhl, Mupcdh, 1810074H01Rik, AI481143
Product # :
PRO-2647Price :
Quantity :
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Shipped with Ice Packs
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Description
CDHR5 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 621 amino acids (29-641 a.a) and having a molecular mass of 66.3kDa.CDHR5 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The CDHR5 solution (0.25mg/1ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CDHR5, also referred to ascadherin-related family member 5, is a calcium-dependent cell adhesion protein. CDHR5 is located in coated pits, and is expressed during lung and kidney developmentat at the lateral and basal surfaces of epithelia.
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Synonyms
Cadherin-related family member 5, Mu-protocadherin, Cdhr5, Mucdhl, Mupcdh, 1810074H01Rik, AI481143
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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
QTQVCSVNQT IFRVEENTTV SEPLVNIFVP DGLHVTLGPL STPYAFRIEG KDLFLNVTPD YEENSLLQAD VECKRGDAVV VRLEVFVAVL DINDNAPKFS FEIKTFNVSE DTKVNTTVIP ETQLKATDAD INDILVYTLQ EVTPNASKFF SLEGVNYPAL KLDQTLDYFK NQNMTFMLLA RDTWEENVEP SHTATATLVL NTLPADLRTP WFLPCSFTDG YVCIHAQYSA VVPTGHKLPS PLIMSPGPIY AVDGDQAINQ SIIYSIIAGN TDGTFIINAH DGNLTMTKSI PSPMKFTLLI RADQEDMAQY SVTQAIVEAR SVTGNPLQFS QSLYYGTVVL GSEAGTAVKD KTFPSEILRI QAQYPGFPDL NSAVTYRVTN SSEFMMNKDI MLTAVPMEEA RTIRVEVEAS NTVTKDTATA VVEIQVSERE LPSTEFPTPP EAGGTTGPSS NTTMEAPLTS GTSQRPATTS SGGSVGPFPP GGTTLRPPTP ASSIPGGSPT LGTSTSPQTT TPGGDSAQTP KPGTSHPTAP TSRTSTSLMT TSSRSDSTQT PKPGTSQPMV PIPGASTSSQ PATPSGSSPQ TPKPGTSQST ATGPISGAGE QGDGQRFSTV DMALEHHHHH H
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
FSH Human, CHODescription:
Follicle Stimulating Hormone Human Recombinant, CHO
Follitropin subunit beta, Follicle-stimulating hormone beta subunit, FSH-beta, FSH-B, Follitropin beta chain, FSH.
Product # :
HOR-067Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
FSH Human Recombinant produced in CHO cells is heterodimeric, glycosylated, polypeptide chain transfected with two expression plasmids encoding the human FSH-alpha chain (Accession # P01215) containing 92 amino and human FSH beta chain containing 111 amino acids (Accession # P01225) having a Mw of 33 kDa.
FSH human recombinant is purified by proprietary chromatographic techniques.
Source
CHO Cells
Formulation
The recombinant FSH was lyophilized from 0.2µm filtered solution containing PBS, pH 7.4.
Purity
Greater than 97% by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
Determined by calf testes membrane, binding characteristics to the testicular FSH receptor which was found to be 25 200 pg/mL.More Info
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Introduction
Follicle stimulating hormone (FSH) is a hormone synthesised and secreted by gonadotropes in the anterior pituitary gland. FSH and LH act synergistically in reproduction: In women, in the ovary FSH stimulates the growth of immature Graafian follicles to maturation. As the follicle grows it releases inhibin, which shuts off the FSH production. In men, FSH enhances the production of androgen-binding protein by the Sertoli cells of the testes and is critical for spermatogenesis. In both males and females, FSH stimulates the maturation of germ cells. In females, FSH initiates follicular growth, specifically affecting granulosa cells. With the concomitant rise in inhibin B FSH levels then decline in the late follicular phase. This seems to be critical in selecting only the most advanced follicle to proceed to ovulation. At the end of the luteal phase, there is a slight rise in FSH that seems to be of importance to start the next ovulatory cycle. Like its partner, LH, FSH release at the pituitary gland is controlled by pulses of gonadotropin-releasing hormone (GnRH). Those pulses, in turn, are subject to the estrogen feed-back from the gonads.
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Synonyms
Follitropin subunit beta, Follicle-stimulating hormone beta subunit, FSH-beta, FSH-B, Follitropin beta chain, FSH.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized recombinant FSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FSH 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 Follicle Stimulating Hormone in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
FSH subunit alpha: APDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLR SKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS.
FSH subunit beta: NSCELTNITIAIEKEECRFCISINTTWCAGYCYTRDLVYKDP ARPKIQKTCTFKELVYETVRVPGCAHHADSLYTYPVATQCHCGKCDSDSTDCTVRGLGPSYCSFGEMKE.
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 :
MRPS25 HumanDescription:
Mitochondrial Ribosomal Protein S25 Human Recombinant
Mitochondrial Ribosomal Protein S25, Mitochondrial 28S Ribosomal Protein S25, 28S Ribosomal Protein S25 Mitochondrial, MRP-S25, RPMS25, S25mt.
Product # :
PRO-1558Price :
Quantity :
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Shipped with Ice Packs
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Description
MRPS25 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (1-173) and having a molecular mass of 22.5kDa.MRPS25 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MRPS25 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MRPS25, a 28S subunit protein, is a member of the ribosomal protein S5P family. An equivalent pseudogene is located on chromosome 4.
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Synonyms
Mitochondrial Ribosomal Protein S25, Mitochondrial 28S Ribosomal Protein S25, 28S Ribosomal Protein S25 Mitochondrial, MRP-S25, RPMS25, S25mt.
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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 MGSMPMKGRF PIRRTLQYLS QGNVVFKDSV KVMTVNYNTH GELGEGARKF VFFNIPQIQY KNPWVQIMMF KNMTPSPFLR FYLDSGEQVL VDVETKSNKE IMEHIRKILG KNEETLREEE EEKKQLSHPA NFGPRKYCLR ECICEVEGQV PCPSLVPLPK EMRGKYKAAL KADAQD
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 :
SlyD E.ColiDescription:
FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase E.Coli Recombinant
FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase, SlyD.
Product # :
ENZ-338Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SlyD Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 196 amino acids and having a molecular mass of 21 kDa.
Source
Escherichia Coli.
Formulation
SlyD protein solution contains 20mM Tris pH-7.5.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Specific activity is > 220 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.More Info
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Introduction
SlyD accessiton#: NP_755987 is a putative folding helper protein from the Escherichia coli cytosol, which has N-terminal prolyl isomerase domain of the FKBP type and a most likely unstructured C-terminal tail. SlyD is an important factor in the biosynthesis of the metal cluster in the [NiFe]-hydrogenase enzymes, and exhibits several activities including that of a peptidyl-prolyl isomerase.
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Synonyms
FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase, SlyD.
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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).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MKVAKDLVVS LAYQVRTEDG VLVDESPVSA PLDYLHGHGS LISGLETALE GHEVGDKFDV AVGANDAYGQ YDENLVQRVP KDVFMGVDEL QVGMRFLAET DQGPVPVEIT AVEDDHVVVD GNHMLAGQNL KFNVEVVAIR EATEEELAHG HVHGAHDHHH DHDHDGCCGG HGHDHGHEHG GEGCCGGKGN GGCGCH.
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 :
EED HumanDescription:
Embryonic Ectoderm Development Human Recombinant
Embryonic ectoderm development, HEED; WAIT1, Polycomb protein EED, hEED, WD protein associating with integrin cytoplasmic tails 1, EED.
Product # :
PRO-1503Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EED Human Recombinant produced in E. coli is a single polypeptide chain containing 464 amino acids (1-441) and having a molecular mass of 52.6kDa. EED is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EED solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
EED is a part of the Polycomb-group family whose members form multimeric protein complexe that are involved in preserving the transcriptional repressive state of genes over successive cell generations. EED mediates repression of gene activity through histone deacetylation, and acts as a specific regulator of integrin function. EED protein interacts with enhancer of zeste 2, the cytoplasmic tail of integrin ?7, immunodeficiency virus type 1 (HIV-1) MA protein, and histone deacetylase proteins.
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Synonyms
Embryonic ectoderm development, HEED; WAIT1, Polycomb protein EED, hEED, WD protein associating with integrin cytoplasmic tails 1, EED.
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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 MGSMSEREVS TAPAGTDMPA AKKQKLSSDE NSNPDLSGDE NDDAVSIESG TNTERPDTPT NTPNAPGRKS WGKGKWKSKK CKYSFKCVNS LKEDHNQPLF GVQFNWHSKE GDPLVFATVG SNRVTLYECH SQGEIRLLQS YVDADADENF YTCAWTYDSN TSHPLLAVAG SRGIIRIINP ITMQCIKHYV GHGNAINELK FHPRDPNLLL SVSKDHALRL WNIQTDTLVA IFGGVEGHRD EVLSADYDLL GEKIMSCGMD HSLKLWRINS KRMMNAIKES YDYNPNKTNR PFISQKIHFP DFSTRDIHRN YVDCVRWLGD LILSKSCENA IVCWKPGKME DDIDKIKPSE SNVTILGRFD YSQCDIWYMR FSMDFWQKML ALGNQVGKLY VWDLEVEDPH KAKCTTLTHH KCGAAIRQTS FSRDSSILIA VCDDASIWRW DRLR.
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 :
BatroxobinDescription:
Batroxobin
Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Batroxobin.
Product # :
PRO-2146Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Batroxobin, isolated from Bothrops atrox snake venom, has an Mw of approximately 43kDa.
Formulation
The Batroxobin protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
More Info
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Introduction
Batroxobin is a serin protease that reduces fibronogen levels and is originally extracted from snake venom of Bothrops Atrox. Batroxobin is used in defibrinogenation and thrombolysis and also has an effect on c-fos gene and growth factor.
Batroxobin can efficiently restrain proliferation of VSMCs, by blocking the release and uptake of Ca2+, thus influencing [Ca2+]i.
Batroxobin converts fibrinogen to fibrin through the restricted release of fibrinopeptide-A from fibrinogen to promote blood to clot. Unlike thrombin, it is not affected by heparin and hirudin. -
Synonyms
Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Batroxobin.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Store the lyophilized Batroxobin between 2-8°C. Do not freeze!
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Solubility
It is recommended to reconstitute the lyophilized Batroxobin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml solutions.
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Unit Definition
100BU [Batroxobin Units]=1mg.
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 :
EIF4A3 HumanDescription:
Eukaryotic Translation Initiation Factor 4A3 Human Recombinant
Eukaryotic initiation factor 4A-III, eIF-4A-III, eIF4A-III, ATP-dependent RNA helicase DDX48, ATP-dependent RNA helicase eIF4A-3, DEAD box protein 48, Eukaryotic initiation factor 4A-like NUK-34, Eukaryotic translation initiation factor 4A isoform 3, Nuclear matrix protein 265, NMP 265, hNMP 265, EIF4A3, DDX48, KIAA0111, NUK34, NMP265, eIF4AIII.
Product # :
PRO-1007Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EIF4A3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 435 amino acids (1-411 a.a.) and having a molecular mass of 49.4kDa. EIF4A3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EIF4A3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 30% glycerol and 200mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Eukaryotic initiation factor 4A-III (EIF4A3) is a member of the DEAD box helicase family and eIF4A subfamily. DEAD box proteins, distinguished by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. These proteins are involved in several cellular processes including alteration of RNA secondary structure, such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. EIF4A3 is a part of a splicing-dependent multiprotein exon junction complex (EJC) accumulated at splice junction on mRNAs. Based upon their distribution patterns, some members of the DEAD box helicase family are thought to be involved in embryogenesis, spermatogenesis, and cellular growth and division.
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Synonyms
Eukaryotic initiation factor 4A-III, eIF-4A-III, eIF4A-III, ATP-dependent RNA helicase DDX48, ATP-dependent RNA helicase eIF4A-3, DEAD box protein 48, Eukaryotic initiation factor 4A-like NUK-34, Eukaryotic translation initiation factor 4A isoform 3, Nuclear matrix protein 265, NMP 265, hNMP 265, EIF4A3, DDX48, KIAA0111, NUK34, NMP265, eIF4AIII.
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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 MGSHMATTAT MATSGSARKR LLKEEDMTKV EFETSEEVDV TPTFDTMGLR EDLLRGIYAY GFEKPSAIQQ RAIKQIIKGR DVIAQSQSGT GKTATFSISV LQCLDIQVRE TQALILAPTR ELAVQIQKGL LALGDYMNVQ CHACIGGTNV GEDIRKLDYG QHVVAGTPGR VFDMIRRRSL RTRAIKMLVL DEADEMLNKG FKEQIYDVYR YLPPATQVVL ISATLPHEIL EMTNKFMTDP IRILVKRDEL TLEGIKQFFV AVEREEWKFD TLCDLYDTLT ITQAVIFCNT KRKVDWLTEK MREANFTVSS MHGDMPQKER ESIMKEFRSG ASRVLISTDV WARGLDVPQV SLIINYDLPN NRELYIHRIG RSGRYGRKGV AINFVKNDDI RILRDIEQYY STQIDEMPMN VADLI.
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 :
EIF4EBP2 HumanDescription:
Eukaryotic Translation Initiation Factor 4E-Binding Protein 2 Human Recombinant
Eukaryotic Translation Initiation Factor 4E Binding Protein 2, 4E-BP2, eIF4E-binding protein 2, 4EBP2, PHASII, phosphorylated.
Product # :
PRO-176Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EIF4EBP2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140amino acids (1-120a.a.) and having a molecular mass of 15.1 kDa. EIF4EBP2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF4EBP2 protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
EIF4EBP2 belongs to the eukaryotic translation initiation factor 4E binding protein family. Even though EIF4EBP2 protein binds eIF4E and inhibits translation initiation, growth factors can release this inhibition by a phosphorylation-dependent disruption. EIF4EBP2 mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase pathway. Regulation of this protein is associated to cell proliferation, cell differentiation and viral infection.
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Synonyms
Eukaryotic Translation Initiation Factor 4E Binding Protein 2, 4E-BP2, eIF4E-binding protein 2, 4EBP2, PHASII, phosphorylated.
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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 MSSSAGSGHQ PSQSRAIPTR TVAISDAAQL PHDYCTTPGG TLFSTTPGGT RIIYDRKFLL DRRNSPMAQT PPCHLPNIPG VTSPGTLIED SKVEVNNLNN LNNHDRKHAV GDDAQFEMDI.
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 :
EMAP II HumanDescription:
Endothelial-Monocyte Activating Polypeptide II Human Recombinant
AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.
Product # :
CYT-607Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
EMAP-II Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 18.3 kDa. The EMAP-II is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium Phosphate buffer pH=7.5 and 130mM sodium chloride.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.More Info
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Introduction
EMAP-II also called SCYE1 is a tumor derived cytokine that plays a role in a wide variety of activities on endothelial cells, monocytes and neutrophils. EMAP-II inhibits endothelial cell proliferation, vasculogenesis, neovessel formation, and can induce apoptosis. It is also chemotactic towards neutrophils and monocytes and induces myeloperoxidase activity from neutrophils. EMAP-II clinical value is inhibiting angiogenesis of vascular beds and suppressing the growth of primary and secondary tumors with no affect to normal tissues. SCYE1is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of this SCYE1 renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor protein is identical to the p43 subunit, which is associated with the multi-tRNA synthetase complex, and it modulates aminoacylation activity of tRNA synthetase in normal cells. EMAP-2 plays a role in in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.
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Synonyms
AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EMAP-II although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EMAP-II 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 EMAP-II 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
SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
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Background
What is the molecular weight/Mw of EMAP II HUMAN Protein?
EMAP II HUMAN Protein has a total Mw of 18.3kDa.
What is the source or expression system of EMAP II HUMAN Protein?
Escherichia Coli.
What is the Purity of EMAP II HUMAN Protein?
EMAP II HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EMAP II HUMAN Protein?
Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.
What is the amino acid sequence of EMAP II HUMAN Protein?
SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
What applications can EMAP II HUMAN Protein be used in?
EMAP II HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EMAP II HUMAN Protein?
The endotoxin level is minimal, EMAP II 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 :
SRI HumanDescription:
Sorcin Human Recombinant
Sorcin, 22 kDa protein, CP-22, CP22, V19, SRI, SCN, FLJ26259.
Product # :
PRO-166Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SRI 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 221 amino acids (1-198 a.a.) and having a molecular mass of 24.1kDa. The SRI is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SRI solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.2M NaCl, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Sorcin (SRI) which is a 22kDa calcium-binding protein was originally identified in multidrug-resistant cells. Sorcin, which modulates excitation-contraction coupling in the heart, contributes to calcium homeostasis in the heart sarcoplasmic reticulum.
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Synonyms
Sorcin, 22 kDa protein, CP-22, CP22, V19, SRI, SCN, FLJ26259.
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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 MGSMAYPGHP GAGGGYYPGG YGGAPGGPAF PGQTQDPLYG YFAAVAGQDG QIDADELQRC LTQSGIAGGY KPFNLETCRL MVSMLDRDMS GTMGFNEFKE LWAVLNGWRQ HFISFDTDRS GTVDPQELQK ALTTMGFRLS PQAVNSIAKR YSTNGKITFD DYIACCVKLR ALTDSFRRRD TAQQGVVNFP YDDFIQCVMS 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 :
STEAP4 HumanDescription:
STEAP Family Member 4 Human Recombinant
DKFZp666D049, FLJ23153, STAMP2, TIARP, TNFAIP9, Six-transmembrane epithelial antigen of prostate 4, SixTransMembrane protein of prostate 2, Tumor necrosis factor, alpha-induced protein 9.
Product # :
PRO-1893Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
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Description
STEAP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-152 a.a) and having a molecular mass of 20.6kDa.STEAP4 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STEAP4 protein solution (1mg/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
STEAP Family Member 4 (STEAP4) is a member of the STEAP (six transmembrane epithelial antigen of prostate) family, resides in the golgi apparatus. STEAP4 act as a metalloreductase which has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+),using NAD(+) as acceptor. According to studies in mice and human it is possible that STEAP4 may involve in adipocyte development and metabolism, and also contribute to the normal biology of the prostate cell.
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Synonyms
DKFZp666D049, FLJ23153, STAMP2, TIARP, TNFAIP9, Six-transmembrane epithelial antigen of prostate 4, SixTransMembrane protein of prostate 2, Tumor necrosis factor, alpha-induced protein 9.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMEKT CIDALPLTMN SSEKQETVCI FGTGDFGRSL GLKMLQCGYS VVFGSRNPQK TTLLPSGAEV LSYSEAAKKS GIIIIAIHRE HYDFLTELTE VLNGKILVDI SNNLKINQYP ESNAEYLAHL VPGAHVVKAF NTISAWALQS GALDASRQ.
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 :
BMP 2 Human, MonomerDescription:
Bone Morphogenetic Protein-2 Human Recombinant, Monomer
BMP-2, BMP2A, Bone morphogenetic protein 2, BMP-2A, BMP2.
Product # :
CYT-627Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Bone Morphogenetic Protein-2 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 115 amino acids (283-396) and having a molecular mass of 13009 Dalton. The BMP-2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-2 solution contains 10mM NaAc pH=3.5 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.
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Synonyms
BMP-2, BMP2A, Bone morphogenetic protein 2, BMP-2A, BMP2.
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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. Please avoid freeze thaw cycles.
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Amino Acid Sequence
MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISMLYLDENEKVV LKNYQDMVVE GCGCR.
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Background
What is the molecular weight/Mw of BMP2 Protein?
BMP2 Protein has a total Mw of 13kDa.
What is the source or expression system of BMP2 Protein?
Escherichia Coli.
What is the Purity of BMP2 Protein?
BMP2 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP2 Protein?
The biological functionality of BMP2 Protein will be determined in the future.
What is the amino acid sequence of BMP2 Protein?
MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISMLYLDENEKVV LKNYQDMVVE GCGCR.
What applications can BMP2 Protein be used in?
BMP2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP2 Protein?
The endotoxin level is minimal, BMP2 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 :
Stratifin HumanDescription:
Tyr-3/Trp- 5 Monooxygenase Activation Protein Sigma Human Recombinant
14-3-3 protein sigma, Epithelial cell marker protein 1, HME1, Stratifin, YWHAS, SFN, Stratifin.
Product # :
PKA-357Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
Stratifin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 248 amino acids (1-248) and having a molecular mass of 27.7 kDa. Stratifin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Stratifin solution containing 20mM Tris-HCl pH-8, 50mM NaCl and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Stratifin is part of the 14-3-3 family. The 14-3-3 family of proteins plays an important regulatory function in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are 7 isoforms, beta, gamma, epsilon, sigma, zeta, tau and eta that have been identified in mammals. Stratifin is an epithelial cell marker that functions as a tumor suppressor whose expression can be down regulated via methylation. Failure of Stratifin expression results in a defective G2/M phase checkpoint and results in epithelial and non-epithelial tumorigenesis.
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Synonyms
14-3-3 protein sigma, Epithelial cell marker protein 1, HME1, Stratifin, YWHAS, SFN, Stratifin.
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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
MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL GLLDSHLIKE AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG EAPQEPQS.
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 Human, HisDescription:
Epiregulin Human Recombinant, His Tag
Epiregulin, Proepiregulin, ER, ERP.
Product # :
CYT-859Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
EREG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 69 amino acids (63-108 a.a) and having a molecular mass of 7.7kDa. EREG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EREG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE
sds-page
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
Epiregulin, Proepiregulin, ER, ERP.
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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 MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.
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Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 7.7kDa.
What is the source or expression system of EREG Protein?
Escherichia Coli.
What is the Purity of EREG Protein?
EREG Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
The biological functionality of EREG Protein will be determined in the future.
What is the amino acid sequence of EREG Protein?
MGSSHHHHHH SSGLVPRGSH MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.
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.