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542 results found for “cell division cycle”
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Name :
CLEC2B Human, Sf9Description:
C-type Lectin Domain Family 2, Member B Human Recombinant, Sf9
C-Type Lectin Domain Family 2 Member B, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 2 (Activation-Induced), IFN-Alpha-2b-Inducing-Related Protein 1, C-Type Lectin Superfamily Member 2, Activation-Induced C-Type Lectin, CLECSF2, IFNRG1, AICL, C-Type Lectin Domain Family 2 Member B, IFN-Alpha2b-Inducing Related Protein 1, HP10085.
Product # :
PRO-2542Price :
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Description
CLEC2B produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 366 amino acids (26-149a.a.) and having a molecular mass of 41.7kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CLEC2B is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques
Source
Sf9, Baculovirus cells.
Formulation
CLEC2B protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
C-type Lectin Domain Family 2, Member B (CLEC2B) belongs to the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Members of the CTL/CTLD family share a common protein fold and have various functions, such as cell adhesion, cell-cell signaling, glycoprotein turnover, and roles in inflammation and immune response. The CLEC2B gene is closely connected to other CTL/CTLD superfamily members on chromosome 12p13 in the natural killer gene complex region. CLEC2B is expressed preferentially in lymphoid tissues, and in most hematopoietic cell types.
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Synonyms
C-Type Lectin Domain Family 2 Member B, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 2 (Activation-Induced), IFN-Alpha-2b-Inducing-Related Protein 1, C-Type Lectin Superfamily Member 2, Activation-Induced C-Type Lectin, CLECSF2, IFNRG1, AICL, C-Type Lectin Domain Family 2 Member B, IFN-Alpha2b-Inducing Related Protein 1, HP10085.
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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
ADPKLTRDSQ SLCPYDWIGF QNKCYYFSKE EGDWNSSKYN CSTQHADLTI IDNIEEMNFL RRYKCSSDHW IGLKMAKNRT GQWVDGATFT KSFGMRGSEG CAYLSDDGAA TARCYTERKW ICRKRIHLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PCK1 HumanDescription:
Phosphoenolpyruvate Carboxykinase 1 Human Recombinant
Phosphoenolpyruvate carboxykinase 1 (soluble), PEPCK-C, PEPCK1, PEP carboxykinase, phosphoenolpyruvate carboxykinase cytosolic [GTP], EC 4.1.1.32.
Product # :
PKA-018Price :
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Description
PCK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 646 amino acids (1-622) and having a molecular mass of 71.7kDa.PCK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PCK1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PCK1 is a central regulating point for the regulation of gluconeogenesis. PCK1 has a vital part in this process by stimulating hepatic glucose production. The expression of PCK1 is controlled by cAMP, glucocorticoids, diet etc. Modulation of the signals controlling PCK1 levels offers a possible therapeutic tactic to the treatment of Diabetes and subsequently obesity.
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Synonyms
Phosphoenolpyruvate carboxykinase 1 (soluble), PEPCK-C, PEPCK1, PEP carboxykinase, phosphoenolpyruvate carboxykinase cytosolic [GTP], EC 4.1.1.32.
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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 MGSHMPPQLQ NGLNLSAKVV QGSLDSLPQA VREFLENNAE LCQPDHIHIC DGSEEENGRL LGQMEEEGIL RRLKKYDNCW LALTDPRDVA RIESKTVIVT QEQRDTVPIP KTGLSQLGRW MSEEDFEKAF NARFPGCMKG RTMYVIPFSM GPLGSPLSKI GIELTDSPYV VASMRIMTRM GTPVLEALGD GEFVKCLHSV GCPLPLQKPL VNNWPCNPEL TLIAHLPDRR EIISFGSGYG GNSLLGKKCF ALRMASRLAK EEGWLAEHML VLGITNPEGE KKYLAAAFPS ACGKTNLAMM NPSLPGWKVE CVGDDIAWMK FDAQGHLRAI NPENGFFGVA PGTSVKTNPN AIKTIQKNTI FTNVAETSDG GVYWEGIDEP LASGVTITSW KNKEWSSEDG EPCAHPNSRF CTPASQCPII DAAWESPEGV PIEGIIFGGR RPAGVPLVYE ALSWQHGVFV GAAMRSEATA AAEHKGKIIM HDPFAMRPFF GYNFGKYLAH WLSMAQHPAA KLPKIFHVNW FRKDKEGKFL WPGFGENSRV LEWMFNRIDG KASTKLTPIG YIPKEDALNL KGLGHINMME LFSISKEFWE KEVEDIEKYL EDQVNADLPC EIEREILALK QRISQM.
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 :
TGFBI HumanDescription:
Transforming Growth Factor Beta Induced Human Recombinant
Transforming growth factor-beta-induced protein ig-h3, Beta ig-h3, Kerato-epithelin, RGD-containing collagen-associated protein, RGD-CAP, TGFBI, BIGH3, CSD, CDB1, CDG2, CSD1, CSD2, CSD3, EBMD, LCD1, CDGG1.
Product # :
PRO-568Price :
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Description
TGFBI Human Recombinant produced in e.Coli is a single, non-glycosylated, polypeptide containing 135 amino acids (502-636) and having a molecular mass of 14.5 kDa. The TGFBI recombinant Human protein is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TGFBI recombinant Human is formulated 20mM Tris-HCl pH-8.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Transforming Growth Factor Beta Induced protein also known as TGFBI is an extracellular matrix protein induced by transforming growth factor (TGF)-beta 1. TGFBI protein is involved in cell growth, cell differentiation, wound healing and cell adhesion. In addition, some missense mutations of TGFBI were identified in families affected with human autosomal dominant corneal dystrophies. TGFBI gene encodes for a 683 amino-acid protein containing an RGD motif and four internal repeated domains which have highly conserved sequences founded in several species (Fasciclin domain).
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Synonyms
Transforming growth factor-beta-induced protein ig-h3, Beta ig-h3, Kerato-epithelin, RGD-containing collagen-associated protein, RGD-CAP, TGFBI, BIGH3, CSD, CDB1, CDG2, CSD1, CSD2, CSD3, EBMD, LCD1, CDGG1.
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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 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
MGTVMDVLKG DNRFSMLVAA IQSAGLTETL NREGVYTVFA PTNEAFRALP PRERSRLLGD AKELANILKY HIGDEILVSG GIGALVRLKS LQGDKLEVSL KNNVVSVNKE PVAEPDIMAT NGVVHVITNV LQPPA.
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 :
S100A8 Human, His-MycDescription:
S100 Calcium Binding Protein A8, His-Myc Tag Human Recombinant
S100 Calcium Binding Protein A8, S100 Calcium-Binding Protein A8 (Calgranulin A), Migration Inhibitory Factor-Related Protein 8, Leukocyte L1 Complex Light Chain , Urinary Stone Protein Band A, Calprotectin L1L Subunit, Cystic Fibrosis Antigen, Calgranulin-A, MRP8, CAGA, CFAG, P8, S100 Calcium Binding Protein A8 (Calgranulin A), S100 Calcium-Binding Protein A8, Calgranulin A, 60B8AG, CP-10, MA38, MRP-8, CGLA, L1Ag, MIF, NIF.
Product # :
PRO-2329Price :
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Description
S100A8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 127 amino acids (1-93) and having a molecular mass of 14.5kDa. S100A8 is fused to a 24 aa His-tag at N-terminus and to a 10 aa Myc-tag at C-terminus.
Source
Escherichia Coli.
Formulation
The S100A8 solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
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Synonyms
S100 Calcium Binding Protein A8, S100 Calcium-Binding Protein A8 (Calgranulin A), Migration Inhibitory Factor-Related Protein 8, Leukocyte L1 Complex Light Chain , Urinary Stone Protein Band A, Calprotectin L1L Subunit, Cystic Fibrosis Antigen, Calgranulin-A, MRP8, CAGA, CFAG, P8, S100 Calcium Binding Protein A8 (Calgranulin A), S100 Calcium-Binding Protein A8, Calgranulin A, 60B8AG, CP-10, MA38, MRP-8, CGLA, L1Ag, MIF, NIF.
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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 MGSHMLTELE KALNSIIDVY HKYSLIKGNF HAVYRDDLKK LLETECPQYI RKKGADVWFK ELDINTDGAV NFQEFLILVI KMGVAAHKKS HEESHKEEQK LISEEDL.
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 :
ARF3 HumanDescription:
ADP-Ribosylation Factor 3 Human Recombinant
ADP-ribosylation factor 3, ARF3.
Product # :
PRO-933Price :
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Description
ARF3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.8kDa.ARF3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARF3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ADP-ribosylation factor 3 (ARF3) belongs to the human ARF gene family. This family encodes small guanine nucleotide-binding proteins which stimulate the ADP-ribosyltransferase activity of cholera toxin and have a role in vesicular trafficking and as activators of phospholipase D. ARF3 functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. ARF3 is involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. The ARF3 gene is comprised of 5 exons and 4 introns.
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Synonyms
ADP-ribosylation factor 3, ARF3.
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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 MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK K.
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 :
IHH HumanDescription:
Indian Hedgehog Human Recombinant
Indian hedgehog protein, IHH, HHG-2, BDA1.
Product # :
CYT-195Price :
Quantity :
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Shipped at Room temp
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Description
IHH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8kDa. The IHH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0?g/ml corresponding to a specific activity of 100-334units/mg.Citations
More Info
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Introduction
IHH belongs to the hedgehog family of secreted signaling molecules. Hedgehog proteins are vital regulators of various developmental processes including growth, patterning and morphogenesis. The vertebrate homologues of Hh comprise several proteins including sonic hedgehog (Shh), Indian hedgehog (Ihh), and Desert hedgehog (Dhh). IHH has a specific role in bone growth and differentiation. In addition, IHH is involved in yolk sac vasculogenesis, having a central role in differentiation of epiblast cells into endothelial and red blood cells. IHH mRNA expression is detected in fetal lung, gut, stomach, liver, kidney, pancreas and strongly in cartilage in growth regions of the developing bone. IHH gene mutations cause the brachydactyly type A1 which is characterized by shortening or malformation of the phalanges and also the acrocapitofemoral dysplasia.
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Synonyms
Indian hedgehog protein, IHH, HHG-2, BDA1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IHH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IHH 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 IHH 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
IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.
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Background
What is the molecular weight/Mw of IHH HUMAN Protein?
IHH HUMAN Protein has a total Mw of 19.8kDa.
What is the source or expression system of IHH HUMAN Protein?
Escherichia Coli.
What is the Purity of IHH HUMAN Protein?
IHH HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IHH HUMAN Protein?
Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0?g/ml corresponding to a specific activity of 100-334units/mg.
What is the amino acid sequence of IHH HUMAN Protein?
IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.
What applications can IHH HUMAN Protein be used in?
IHH HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IHH HUMAN Protein?
The endotoxin level is minimal, IHH 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 :
CAPZA2 HumanDescription:
Capping Protein (Actin Filament) Muscle Z-Line Alpha 2 Human Recombinant
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.
Product # :
PRO-1721Price :
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Description
CAPZA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (1-286 a.a) and having a molecular mass of 35.3kDa.CAPZA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CAPZA2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, and 0.4M UREA.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2 also known as CAPZA2 belongs the F-actin capping protein alpha subunit family. It is the alpha subunit of the barbed-end actin binding protein Cap Z. By capping the barbed end of actin filaments, Cap Z regulates the growth of the actin filaments at the barbed end. Among the diseases associated with CAPZA2 are endocarditis, and cervicitis.
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Synonyms
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.
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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 MGSMADLEEQ LSDEEKVRIA AKFIIHAPPG EFNEVFNDVR LLLNNDNLLR EGAAHAFAQY NLDQFTPVKI EGYEDQVLIT EHGDLGNGKF LDPKNRICFK FDHLRKEATD PRPCEVENAV ESWRTSVETA LRAYVKEHYP NGVCTVYGKK IDGQQTIIAC IESHQFQAKN FWNGRWRSEW KFTITPSTTQ VVGILKIQVH YYEDGNVQLV SHKDIQDSLT VSNEVQTAKE FIKIVEAAEN EYQTAISENY QTMSDTTFKA LRRQLPVTRT KIDWNKILSY KIGKEMQNA.
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 :
IL2 Human, YeastDescription:
Interleukin-2 Human Recombinant, Yeast
Interleukin-2, T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2.
Product # :
CYT-797Price :
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Shipping Method :
Shipped at Room temp
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Description
Interleukin-2 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 134 amino acids and having a molecular mass of 14 kDa. The IL-2 is purified by proprietary chromatographic techniques.
Source
Pichia pastoris.
Formulation
The protein was lyophilized from a 0.2µm filtered solution in 20mM sodium phosphate buffer pH 7.0 in absence of any carrier protein.
Purity
Greater than 98% as determined by SDS-PAGE.
Biological Activity
The biological activity is determined by the dose dependent proliferation of mouse CTLL–2 cells. Optimal concentration for individual application should be determined by a dose response assay. ED50 range = 0.08–0.5ng/mlCitations
More Info
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Introduction
IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.
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Synonyms
Interleukin-2, T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Interleukin-2 should be stored at 4C between 2-7 days and for future use below -18C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin-2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
A P T S S S T K K T Q L Q L E H L L L D L Q M I L N G I N N Y K N P K L T R M L T F K F Y M P K K A T E L K H L Q C L E E E L K P L E E V L N L A Q S K N F H L R P R D L I S N I N V I V L E L K G S E T T F M C E Y A D E T A T I V E F L N R W I T F C Q S I I S T L T.
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Background
What is the molecular weight/Mw of IL 2 HUMAN, YEAST Protein?
IL 2 HUMAN, YEAST Protein has a total Mw of 14kDa.
What is the source or expression system of IL 2 HUMAN, YEAST Protein?
Pichia pastoris.
What is the Purity of IL 2 HUMAN, YEAST Protein?
IL 2 HUMAN, YEAST Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of IL 2 HUMAN, YEAST Protein?
The biological activity is determined by the dose dependent proliferation of mouse CTLL–2 cells. Optimal concentration for individual application should be determined by a dose response assay. ED50 range = 0.08–0.5ng/ml
What is the amino acid sequence of IL 2 HUMAN, YEAST Protein?
A P T S S S T K K T Q L Q L E H L L L D L Q M I L N G I N N Y K N P K L T R M L T F K F Y M P K K A T E L K H L Q C L E E E L K P L E E V L N L A Q S K N F H L R P R D L I S N I N V I V L E L K G S E T T F M C E Y A D E T A T I V E F L N R W I T F C Q S I I S T L T.
What applications can IL 2 HUMAN, YEAST Protein be used in?
IL 2 HUMAN, YEAST Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL 2 HUMAN, YEAST Protein?
The endotoxin level is minimal, IL 2 HUMAN, YEAST Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL 2 HUMAN, YEAST that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL 2 HUMAN, YEAST?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
XPA HumanDescription:
Xeroderma Pigmentosum, Complementation Group A Human Recombinant
XP1, XPAC, DNA repair protein complementing XP-A cells.
Product # :
PRO-026Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
XPA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-273 a.a.) and having a molecular mass of 33.8 kDa.XPA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
XPA protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
DNA repair protein complementing XP-A cells, (XPA), is a member of the XPA family. XPA protein takes a part in DNA excision repair. It Inductees repair by binding to damaged sites with different affinities depending on the photoproduct and the transcriptional state of the region. Defects in XPA is the reason of xeroderma pigmentosum complementation group A (XP-A), which is infrequent human autosomal recessive disease which characterized by solar sensitivity, high predisposition for developing cancers on areas exposed to sunlight, also may cause to neurological abnormalities.
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Synonyms
XP1, XPAC, DNA repair protein complementing XP-A cells.
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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 MGSMAAADGA LPEAAALEQP AELPASVRAS IERKRQRALM LRQARLAARP YSATAAAATG GMANVKAAPK IIDTGGGFIL EEEEEEEQKI GKVVHQPGPV MEFDYVICEE CGKEFMDSYL MNHFDLPTCD NCRDADDKHK LITKTEAKQE YLLKDCDLEK REPPLKFIVK KNPHHSQWGD MKLYLKLQIV KRSLEVWGSQ EALEEAKEVR QENREKMKQK KFDKKVKELR RAVRSSVWKR ETIVHQHEYG PEENLEDDMY RKTCTMCGHE LTYEKM .
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 :
DUSP23 Human, ActiveDescription:
Dual Specificity Phosphatase 23 Human Recombinant, Active
Dual specificity protein phosphatase 23, Low molecular mass dual specificity phosphatase 3, LDP-3, VH1-like phosphatase Z, DUSP23, LDP3, VHZ, VH1-Like Member Z, EC 3.1.3.16, EC 3.1.3.48, DUSP25, MOSP, LDP3, Dual Specificity Phosphatase 23, VH1-Like Phosphatase Z, LDP-3, VHZ, Low-Molecular-Mass Dual-Specificity Phosphatase 3, Low Molecular Mass Dual Specificity Phosphatase 3, Dual Specificity Protein, Phosphatase 23, Testicular Tissue Protein Li 59.
Product # :
ENZ-1043Price :
Quantity :
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Description
DUSP23 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-150 a.a) and having a molecular mass of 18.8kDa.DUSP23 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DUSP23 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 200 units/mg, and is defined as the amount of enzyme that hydrolyzes 1.0 nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37°C.
Citations
More Info
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Introduction
DUSP23 is a member of the protein-tyrosine phosphatase family. DUSP23 is a protein phosphatase which facilitates dephosphorylation of phosphorylated proteins on Tyr and Ser/Thr residues. In vitro, DUSP23 dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10). In addition, DUSP23 enhances activation of JNK and p38(MAPK14).
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Synonyms
Dual specificity protein phosphatase 23, Low molecular mass dual specificity phosphatase 3, LDP-3, VH1-like phosphatase Z, DUSP23, LDP3, VHZ, VH1-Like Member Z, EC 3.1.3.16, EC 3.1.3.48, DUSP25, MOSP, LDP3, Dual Specificity Phosphatase 23, VH1-Like Phosphatase Z, LDP-3, VHZ, Low-Molecular-Mass Dual-Specificity Phosphatase 3, Low Molecular Mass Dual Specificity Phosphatase 3, Dual Specificity Protein, Phosphatase 23, Testicular Tissue Protein Li 59.
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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 MGVQPPNFSW VLPGRLAGLA LPRLPAHYQF LLDLGVRHLV SLTERGPPHS DSCPGLTLHR LRIPDFCPPA PDQIDRFVQI VDEANARGEA VGVHCALGFG RTGTMLACYL VKERGLAAGD AIAEIRRLRP GSIETYEQEK AVFQFYQRTK.
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 :
ANXA5 HumanDescription:
Annexin A5 Human Recombinant
PP4, ANX5, ENX2, ANXA5, Annexin A5, Annexin-5, Annexin V, Lipocortin V, Endonexin II, Calphobindin I, CBP-I, Placental anticoagulant protein I, PAP-I, Placental anticoagulant protein 4, Thromboplastin inhibitor, Vascular anticoagulant-alpha, VAC-alpha, Anchorin CII.
Product # :
PRO-732Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ANXA5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-320 a.a.) and having a molecular mass of 35.9 kDa.ANXA5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ANXA5 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ANXA5 is a member of the annexin family of calcium-dependent phospholipid binding proteins which are involved in membrane-related activity along exocytotic and endocytotic pathways. ANXA5 is a phospholipase A2 and protein kinase C inhibitory protein with calcium channel properties and takes part in cellular signal transduction, inflammation, growth and differentiation. ANXA5 is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. ANXA5 regulates coagulability in the blood stream by binding to phosphatidylserine and sulfatide. ANXA5 protects sinsuoidal endothelial cells from ischemia reperfusion damage. ANXA5 is necessary for normal CFTR chloride channel activity.
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Synonyms
PP4, ANX5, ENX2, ANXA5, Annexin A5, Annexin-5, Annexin V, Lipocortin V, Endonexin II, Calphobindin I, CBP-I, Placental anticoagulant protein I, PAP-I, Placental anticoagulant protein 4, Thromboplastin inhibitor, Vascular anticoagulant-alpha, VAC-alpha, Anchorin CII.
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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
MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR QEISAAFKTL FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTNEKVL TEIIASRTPE ELRAIKQVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDAGIDEA QVEQDAQALF QAGELKWGTD EEKFITIFGT RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVMVSRSEID LFNIRKEFRK NFATSLYSMI KGDTSGDYKK ALLLLCGEDD.
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 :
HAVCR1 HumanDescription:
Hepatitis A Virus Cellular Receptor 1 Human Recombinant
Hepatitis A Virus Cellular Receptor 1, T-Cell Immunoglobulin Mucin Family Member 1, T-Cell Immunoglobulin Mucin Receptor 1, T-Cell Membrane Protein 1, Kidney Injury Molecule 1, HAVCR-1, TIMD-1, HAVCR, KIM-1, TIM-1, TIMD1, TIM1, KIM1, TIM, T-Cell Immunoglobulin And Mucin Domain-Containing Protein 1, T Cell Immunoglobin Domain And Mucin Domain Protein 1, HAVCR1.
Product # :
HAV-222Price :
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Description
HAVCR1 Human Recombinant produced in E. coli is a single polypeptide chain containing 298 amino acids (21-295aa) and having a molecular mass of 31.9kDa.HAVCR1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HAVCR1 solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Hepatitis A virus cellular receptor 1 (HAVCR1) is a membrane receptor for both human hepatitis A virus (HHAV) and TIMD4. HAVCR1 is a type I trans-membrane structural glycoprotein located in the renal proximal tubule epithelial cells. HAVCR1 protein may be involved in the control of asthma and allergic diseases. The reference genome represents an allele which retains a MTTVP amino acid segment that presents defense against atopy in HHAV seropositive individuals.
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Synonyms
Hepatitis A Virus Cellular Receptor 1, T-Cell Immunoglobulin Mucin Family Member 1, T-Cell Immunoglobulin Mucin Receptor 1, T-Cell Membrane Protein 1, Kidney Injury Molecule 1, HAVCR-1, TIMD-1, HAVCR, KIM-1, TIM-1, TIMD1, TIM1, KIM1, TIM, T-Cell Immunoglobulin And Mucin Domain-Containing Protein 1, T Cell Immunoglobin Domain And Mucin Domain Protein 1, HAVCR1.
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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 MGSSVKVGGE AGPSVTLPCH YSGAVTSMCW NRGSCSLFTC QNGIVWTNGT HVTYRKDTRY KLLGDLSRRD VSLTIENTAV SDSGVYCCRV EHRGWFNDMK ITVSLEIVPP KVTTTPIVTT VPTVTTVRTS TTVPTTTTVP MTTVPTTTVP TTMSIPTTTT VLTTMTVSTT TSVPTTTSIP TTTSVPVTTT VSTFVPPMPL PRQNHEPVAT SPSSPQPAET HPTTLQGAIR REPTSSPLYS YTTDGNDTVT ESSDGLWNNN QTQLFLEHSL LTANTTKG
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 :
VEGF (121 a.a.) MouseDescription:
Vascular Endothelial Growth Factor (121 a.a.) Mouse Recombinant
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-574Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Vascular Endothelial Growth Factor-121 Mouse Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of 28.4 kDa.Recombinant Mouse VEGF-121 is a truncated version of Murine VEGF-165.The VEGF-121 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized VEGF-121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 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 VEGF-121 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
MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKCDKRPR R.
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 :
RCN2 HumanDescription:
Reticulocalbin 2 Human Recombinant
Reticulocalbin-2, Calcium-binding protein ERC-55, E6-binding protein, 6BP, RCN2, ERC55, E6BP, ERC-55, TCBP49.
Product # :
PRO-189Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RCN2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 313 amino acids (26-317 a.a.) and having a molecular mass of 36.8kDa (Molecular weight on SDS-PAGE will appear higher).RCN2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RCN2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Reticulocalbin-2 (RCN2) is a member of the CREC protein family. RCN2 is a calcium-binding protein found in the lumen of the ER. RCN2 contains 6 conserved regions with similarity to a high affinity Ca(+2)-binding motif, the EF-hand.
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Synonyms
Reticulocalbin-2, Calcium-binding protein ERC-55, E6-binding protein, 6BP, RCN2, ERC55, E6BP, ERC-55, TCBP49.
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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 MEELHYPLGE RRSDYDREAL LGVQEDVDEY VKLGHEEQQK RLQAIIKKID LDSDGFLTES ELSSWIQMSF KHYAMQEAKQ QFVEYDKNSD DTVTWDEYNI QMYDRVIDFD ENTALDDAEE ESFRKLHLKD KKRFEKANQD SGPGLSLEEF IAFEHPEEVD
YMTEFVIQEA LEEHDKNGDG FVSLEEFLGD YRWDPTANED PEWILVEKDR FVNDYDKDND GRLDPQELLP WVVPNNQGIA QEEALHLIDE MDLNGDKKLS EEEILENPDL FLTSEATDYG RQLHDDYFYH DEL.
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 :
Transferrin Human, CHODescription:
Transferrin Human Recombinant, CHO
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Product # :
PRO-2782Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Transferrin produced in CHO cells is a glycosylated, polypeptide chain containing having a molecular mass of 76 kDa. Human Transferrin has homologous C and N-terminal domains, each of which binds one ion of ferric iron.
Source
Chinese Hamster Ovary cells.
Formulation
Transferrin solution contains 0.05% NaN3 and PBS.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
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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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Applications
Immunoassay, cell culture.
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Background
Human recombinant transferrin, a glycoprotein responsible for iron transport in the body, has gained increasing attention in the fields of biomedicine and health sciences. This multifaceted protein serves as an essential carrier of iron and is crucial for cellular growth, immunity, and various physiological processes. Its recombinant form, produced through advanced biotechnological methods, offers several advantages for therapeutic and research purposes. This study aims to provide a comprehensive exploration of human recombinant transferrin, shedding light on its various functions and potential applications in health and biomedicine.
The primary objective of this research is to elucidate the essential role of transferrin in iron homeostasis and its significance for human health. In vitro and in vivo experiments will be conducted to investigate how recombinant transferrin interacts with cellular receptors, regulates iron uptake, and influences cellular proliferation. Understanding these mechanisms is fundamental for deciphering the complexities of iron metabolism and its impact on health and disease.
The second objective is to assess the clinical relevance of human recombinant transferrin in medical interventions. Clinical trials and studies involving individuals with iron-related disorders, such as iron-deficiency anemia, will be conducted to evaluate the efficacy and safety of recombinant transferrin supplementation. These investigations may provide insights into the use of recombinant transferrin as a therapeutic agent in various clinical settings.
The third objective is to explore the broader implications of human recombinant transferrin in biomedicine and research. Research will investigate its potential roles in areas beyond iron transport, such as drug delivery, tissue engineering, and cell culture. Understanding the multifaceted properties of recombinant transferrin may open new avenues for innovative approaches in various medical specialties and scientific research.
By delving into the diverse functions of human recombinant transferrin, this research aims to expand our understanding of its physiological roles and clinical applications. The findings may contribute to the development of innovative strategies for the treatment of iron-related disorders and the advancement of biomedicine and scientific research.
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 :
T.Vaginalis P65 AntibodyDescription:
Polyclonal Rabbit Anti Trichomonas Vaginalis P65 Antibody
Product # :
ANT-494Price :
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Description
The polyclonal antibody to Trichomonas vaginalis was collected from the rabbit igG and immunized with recombinant T. Vaginalis P65.
Formulation
50mM mg glycine, pH8.0.
Purity
Pure Rabbit IgG.
Citations
More Info
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Introduction
Trichomonas vaginalis, an anaerobic, flagellated protozoan parasite, is most dominant protozoan causing sexual transmitted disease. T. vaginalis induced vaginal tract infection occurs as multiple steps involving interactions between host macromolecules and protozoan virulent factor. Adhension protein P65 of T. vaginalis has a vital part in assisting the penetration into vaginal tract surface.
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Physical Appearance
Sterile Filtered clear 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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Purification Method
Purified by affinity chromatographic technique.
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 :
RBP3 HumanDescription:
Retinol Binding Protein-3 Human Recombinant
RBP3, IRBP, Retinol-binding protein 3, Interphotoreceptor retinoid-binding protein, Interstitial retinol-binding protein.
Product # :
CYT-1175Price :
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Shipped at Room temp
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Description
RBP3 Human Recombinant (321-630a.a) produced in E.Coli is a single, non-glycosylated Polypeptide chain. RBP3 is fused to a 6 a.a His tag at N-terminal and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RBP3 was lyophilized from a concentrated 0.2µm solution in PBS pH, 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Retinol-binding proteins (RBP) are a family of proteins with various functions. Retinol and retinoic acid play crucial roles in the modulation of gene expression and overall development of an embryo. However, deficit or excess of either one of these substances can cause early embryo mortality or developmental malformations. Regulation of transport and metabolism of retinol necessary for a successful pregnancy is accomplished via RBP. Retinol binding proteins have been identified within the uterus, embryo, and extraembryonic tissue of the bovine, ovine, and porcine, therefore RBP takes part in proper retinol exposure to the embryo and successful transport at the maternal-fetal interface.
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Synonyms
RBP3, IRBP, Retinol-binding protein 3, Interphotoreceptor retinoid-binding protein, Interstitial retinol-binding protein.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized RBP3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution. Retinol Binding Protein-3 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 RBP3 in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CLTA HumanDescription:
Clathrin, Light Chain A Human Recombinant
Clathrin light chain A, Lca, CLTA.
Product # :
PRO-1144Price :
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Description
CLTA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (1-218 a.a) and having a molecular mass of 26.2kDa (Molecular weight on SDS-PAGE will appear higher).CLTA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CLTA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Clathrin, light chain A (CLTA) is a member of the clathrin family. Clathrin, which is a large, soluble protein, is comprised of heavy and light chains. CLTA is one of 2 clathrin light chain proteins which are supposed to function as regulatory elements. CLTA is a key cytosolic coat protein in pits and vesicles originating from the plasma membrane and the trans-Golgi network. In receptor-mediated endocytosis, receptor proteins are encapsulated by Clathrin-coated vesicles.
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Synonyms
Clathrin light chain A, Lca, CLTA.
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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 MGSHMAELDP FGAPAGAPGG PALGNGVAGA GEEDPAAAFL AQQESEIAGI ENDEAFAILD GGAPGPQPHG EPPGGPDAVD GVMNGEYYQE SNGPTDSYAA ISQVDRLQSE PESIRKWREE QMERLEALDA NSRKQEAEWK EKAIKELEEW YARQDEQLQK
TKANNRAAEE AFVNDIDESS PGTEWERVAR LCDFNPKSSK QAKDVSRMRS VLISLKQAPL VH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SELE Human, HEKDescription:
E-Selectin Human Recombinant, HEK
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.
Product # :
PRO-1645Price :
Quantity :
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Shipped at Room temp
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Description
SELE Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 543 amino acids (22-556). SELE is fused to an 8 amino acid His-tag at C-terminus is purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
SELE was lyophilized from a 0.2 µM filtered solution of PBS and 4% Mannitol, pH 7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.
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Synonyms
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SELE although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SELE should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized SELE in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
WSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILSYSPSYYWIGIRKVNNVW
VWVGTQKPLTEEAKNWAPGEPNNRQKDEDCVEIYIKREKDVGMWNDERCSKKKLALCYTA
ACTNTSCSGHGECVETINNYTCKCDPGFSGLKCEQIVNCTALESPEHGSLVCSHPLGNFSY
NSSCSISCDRGYLPSSMETMQCMSSGEWSAPIPACNVVECDAVTNPANGFVECFQNPGSFPW
NTTCTFDCEEGFELMGAQSLQCTSSGNWDNEKPTCKAVTCRAVRQPQNGSVRCSHSPAGEFT
FKSSCNFTCEEGFMLQGPAQVECTTQGQWTQQIPVCEAFQCTALSNPERGYMNCLPSASGSFR
YGSSCEFSCEQGFVLKGSKRLQCGPTGEWDNEKPTCEAVRCDAVHQPPKGLVRCAHSPIGEFTY
KSSCAFSCEEGFELHGSTQLECTSQGQWTEEVPSCQVVKCSSLAVPGKINMSCSGEPVFGTVCKF
ACPEGWTLNGSAARTCGATGHWSGLLPTCEAPTESNIPVDHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
OLR1 Human, HEKDescription:
Oxidized Low Density Lipoprotein Receptor 1 Human Recombinant, HEK
Oxidized low density lipoprotein (lectin-like) receptor 1, CLEC8A, hLOX1, SCARE1, Lectin-type oxidized LDL receptor 1, Lectin-like oxidized LDL receptor 1, C-type lectin domain family 8 member A, LOXIN, SLOX1, ox LDL receptor 1, Oxidized low-density lipoprotein receptor 1 soluble form, scavenger receptor class E member 1, SR-E1.
Product # :
PRO-2293Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
OLR1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser61-Gln273) containing a total of 221 amino acids, having a calculated molecular mass of 25.3kDa and fused to a 8 aa Flag tag at N-Terminus.
Source
HEK 293.
Formulation
OLR1 was filtered (0.4µm) and lyophilized in phosphate buffered saline pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
OLR1 is a type II membrane protein which belongs to the C-type lectin family and performs as a cell-surface receptor for Ox-LDL. Ox-LDL has a part in early ather-osclerosis, which includes the transformation of monocyte-derived macro-phages to foam cells in atherosclerotic lesions. In addition, OLR1 protein triggers the activation of the NF?B signal transduction pathway.
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Synonyms
Oxidized low density lipoprotein (lectin-like) receptor 1, CLEC8A, hLOX1, SCARE1, Lectin-type oxidized LDL receptor 1, Lectin-like oxidized LDL receptor 1, C-type lectin domain family 8 member A, LOXIN, SLOX1, ox LDL receptor 1, Oxidized low-density lipoprotein receptor 1 soluble form, scavenger receptor class E member 1, SR-E1.
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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 prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture.
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Amino Acid Sequence
DYKDDDDKSQ VSDLLTQEQA NLTHQKKKLE GQISARQQAE EASQESENEL KEMIETLARK LNEKSKEQME LHHQNLNLQE TLKRVANCSA PCPQDWIWHG ENCYLFSSGS FNWEKSQEKC LSLDAKLLKI NSTADLDFIQ QAISYSSFPF WMGLSRRNPS YPWLWEDGSP LMPHLFRVRG AVSQTYPSGT CAYIQRGAVY AENCILAAFS ICQKKANLRA Q.
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 :
FADD HumanDescription:
Fas-Associated Death Domain Human Recombinant
GIG3, MORT1, MGC8528, FADD, Fas (TNFRSF6)-associated via death domain, Protein FADD, FAS-associated death domain protein, FAS-associating death domain-containing protein, Mediator of receptor induced toxicity, Growth-inhibiting gene 3 protein.
Product # :
PRO-733Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FADD produced in E.Coli is a single, non-glycosylated polypeptide chain containing 244 amino acids (1-208 a.a.) and having a molecular mass of 27.4 kDa.FADD is fused to 36 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FADD protein solution contains 20mM Tris-HCl, pH-8, and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
FADD is an adaptor protein that cooperates with a variety of cell surface receptors and mediates cell apoptotic signals. Using its C-terminal death domain, FADD is recruited by TNFRSF6/Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TNFSF10/TRAIL-receptor, and consequently it take parts in the death signaling initiated by these receptors. FADD interaction with the receptors reviels the N-terminal effector domain of, which allows it to recruit caspase-8, and thus initiate the cysteine protease cascade. Knockout studies in mice furthermore propose the significance of FADD in premature T cell development. FADD plays a role in survival/proliferation and cell cycle development. FADD also takes part in cellular sublocalization, protein phosphorylation, and inhibitory molecules.
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Synonyms
GIG3, MORT1, MGC8528, FADD, Fas (TNFRSF6)-associated via death domain, Protein FADD, FAS-associated death domain protein, FAS-associating death domain-containing protein, Mediator of receptor induced toxicity, Growth-inhibiting gene 3 protein.
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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
MRGSHHHHHHGMASMTGGQQ MGRDLYDDDD KDRWGSMDPF LVLLHSVSSS LSSSELTELK FLCLGRVGKR KLERVQSGLD LFSMLLEQND LEPGHTELLR ELLASLRRHD LLRRVDDFEA GAAAGAAPGE EDLCAAFNVI CDNVGKDWRR LARQLKVSDT KIDSIEDRYP RNLTERVRES LRIWKNTEKE NATVAHLVGA LRSCQMNLVA DLVQEVQQAR DLQNRSGAMS PMSWNSDAST SEAS.
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 :
LIF HumanDescription:
Leukemia Inhibitory Factor Human Recombinant
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Product # :
CYT-644Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leukemia Inhibitory Factor (LIF) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the M1 cell differentiation assay is < 0.01 ng/ml, corresponding to a specific activity of 100,000,000IU/mg.Citations
More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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 Leukemia Inhibitory Factor (LIF) 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
SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF.
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Background
Leukemia Inhibitory Factor (LIF) Background
Leukemia Inhibitory Factor (LIF) is a cytokine within the interleukin-6 family. It is influential in the hypothalamus and involved in energy balance.
LIF stimulates ACTH secretion and affects the stress and immune response in the body. Administration of LIF has been shown to correct low plasma ACTH and repair hypothalamic-pituitary-adrenal (HPA) axis responses.
Function and Applications of LIF
LIF prevents the proliferation of myeloid leukemia cells by inducing their terminal differentiation. Beyond cancer, LIF influences bone metabolism, embryogenesis, and inflammation.
Moreover, it supports the self-renewal of stem cells in culture by activating Stat3, thus preventing spontaneous differentiation, and is studied for potential benefits in fertility treatments.
Structure and Interactions
LIF's structure consists of a four alpha-helix bundle similar to other hematopoietic cytokines. It interacts with components such as the ciliary neurotrophic factor (CNTF) through multimeric receptors, influencing both cytokine's effects on cells. This interaction is crucial for forming high-affinity binding sites that mediate their biological activities.
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 :
ISOC2 HumanDescription:
Isochorismatase Domain Containing 2 Human Recombinant
Isochorismatase domain-containing protein 2, mitochondrial, ISOC2, Isochorismatase Domain Containing 2.
Product # :
PRO-1669Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ISOC2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (59-205) and having a molecular mass of 18kDa.ISOC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ISOC2 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.
Citations
More Info
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Introduction
Isochorismatase Domain Containing 2, also known as ISOC2, is a part of the isochorismatase family. SOC2 is localized in mitochondrion, cytoplasm, and nucleus. ISOC2 which interacts with CDKN2A is localizes to the nucleus in the attendance of CDKN2A.
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Synonyms
Isochorismatase domain-containing protein 2, mitochondrial, ISOC2, Isochorismatase Domain Containing 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 MGSEQYPQGL GPTVPELGTE GLRPLAKTCF SMVPALQQEL DSRPQLRSVL LCGIEAQACI LNTTLDLLDR GLQVHVVVDA CSSRSQVDRL VALARMRQSG AFLSTSEGLI LQLVGDAVHP QFKEIQKLIK EPAPDSGLLG LFQGQNSLLH.
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 :
FAM3C HumanDescription:
Family with Sequence Similarity 3, Member C Human Recombinant
Family with sequence similarity 3 member C, ILEI, Interleukin-like EMT inducer, predicted osteoblast protein, GS3876, protein FAM3C.
Product # :
PRO-952Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FAM3C Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (25-227) and having a molecular mass of 24.5 kDa.FAM3C is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The FAM3C solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 200mM NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
FAM3C is a member of the FAM3 family and holds a GG domain. Pancreatic cancer-derived cells demonstrate a difference in expression of this protein. FAM3C is a downstream target gene for the Nkx5-1 transcription factor, and there for takes part in cell differentiation and proliferation through inner ear embryogenesis. In addition, FAM3C has a role in retinal laminar formation and promotes epithelial to mesenchymal transition.
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Synonyms
Family with sequence similarity 3 member C, ILEI, Interleukin-like EMT inducer, predicted osteoblast protein, GS3876, protein FAM3C.
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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 MQVFEIKMDA SLGNLFARSA LDTAARSTKP PRYKCGISKA CPEKHFAFKM ASGAANVVGP KICLEDNVLM SGVKNNVGRG INVALANGKT GEVLDTKYFD MWGGDVAPFI EFLKAIQDGT IVLMGTYDDG ATKLNDEARR LIADLGSTSI TNLGFRDNWV FCGGKGIKTK SPFEQHIKNN KDTNKYEGWP EVVEMEGCIP QKQD
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.