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1000 results found for “DNA-Damage Protein”
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Name :
NSL1 HumanDescription:
NSL1 Human Recombinant
NSL1 MIS12 Kinetochore Complex Component, NSL1 MIND Kinetochore Complex Component Homolog (S. Cerevisiae), Kinetochore-Associated ProteinNSL1 Homolog, Chromosome 1 Open Reading Frame 48, C1orf48, MIS14.
Product # :
PRO-1557Price :
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Description
NSL1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (1-281) and having a molecular mass of 34.6kDa.NSL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NSL1 solution (1mg/ml) 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
NSL1 holds two coiled-coil domains.NSL1 proteins, localized to kinetochores - chromosome associated structures which attach to microtubules and mediate chromosome movements throughout cell division. NSL1 is a fragment of a conserved protein complex that hold two chromodomain-containing proteins and a component of the outer plate of the kinetochore. NSL1 connect centromeric heterochromatin with the outer kinetochore structure. Several transcript variants are known to encod different isoforms for this gene.
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Synonyms
NSL1 MIS12 Kinetochore Complex Component, NSL1 MIND Kinetochore Complex Component Homolog (S. Cerevisiae), Kinetochore-Associated ProteinNSL1 Homolog, Chromosome 1 Open Reading Frame 48, C1orf48, MIS14.
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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 MGSMAGSPEL VVLDPPWDKE LAAGTESQAL VSATPREDFR VRCTSKRAVT EMLQLCGRFV QKLGDALPEE IREPALRDAQ WTFESAVQEN ISINGQAWQE ASDNCFMDSD IKVLEDQFDE IIVDIATKRK QYPRKILECV IKTIKAKQEI LKQYHPVVHP LDLKYDPDPA PHMENLKCRG ETVAKEISEA MKSLPALIEQ GEGFSQVLRM QPVIHLQRIH QEVFSSCHRK PDAKPENFIT QIETTPTETA SRKTSDMVLK RKQTKDCPQR KWYPLRPKKI NLDT
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 :
FHIT HumanDescription:
Fragile Histidine Triad Human Recombinant
EC 3.6.1.29, Dinucleosidetriphosphatase, Bis (5''-adenosyl)-triphosphatase , AP3Aase, AP3A hydrolase, Diadenosine 5'',5''''''-P1,P3-triphosphate hydrolase, FRA3B.
Product # :
PRO-828Price :
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Description
FHIT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids (1-147 a.a.) and having a molecular mass of 17.9 kDa. FHIT protein is fused to an 8 amino acid His tag at C-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
FHIT Human solution containing 20mM Tris-HCl pH-8 & 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
FHIT enzyme cleaves adenosine 5'' PPP 5'' A to yield AMP and ADP. FHIT gene includees the regular fragile site FRA3B on chromosome 3. Alterations and deletions of the FHIT gene are highly linked to the genesis and establishment of human tumors of the lung, cervix, breast, colon, stomach and pancreas. In normal cells, FHIT functions as a tumor suppressor and physically relates with ubiquitin conjugating enzyme 9.
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Synonyms
EC 3.6.1.29, Dinucleosidetriphosphatase, Bis (5''-adenosyl)-triphosphatase , AP3Aase, AP3A hydrolase, Diadenosine 5'',5''''''-P1,P3-triphosphate hydrolase, FRA3B.
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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
MSFRFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLVCP LRPVERFHDL RPDEVADLFQ TTQRVGTVVE KHFHGTSLTF SMQDGPEAGQ TVKHVHVHVL PRKAGDFHRN DSIYEELQKH DKEDFPASWR SEEEMAAEAA ALRVYFQLEH HHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MAGEA8 HumanDescription:
Melanoma Antigen Family A, 8 Human Recombinant
Melanoma Antigen Family A8, MAGE-8 Antigen, MAGE8, Cancer/Testis Antigen 1.8, CT1.8, Cancer/Testis Antigen Family 1, Member 8, Cancer/Testis Antigen Family 1, Melanoma-Associated Antigen 8, Melanoma Antigen Family A, 8, Member 8, MAGEA8.
Product # :
PRO-2206Price :
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Description
MAGEA8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (1-318 a.a) and having a molecular mass of 37.6kDa.MAGEA8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MAGEA8 protein solution (0.25mg/ml) containing Phosphate Buffered Saline, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Melanoma Antigen Family A 8, also known as MAGEA8 belongs to the MAGE gene family, which includes twelve known genes, of which six are expressed in tumors. Furthermore, the MAGE genes were at first isolated from different kinds of tumors, and according to their virtually exclusive tumor-specific expression in adult tissues, they have been used as targets for cancer immunotherapy.
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Synonyms
Melanoma Antigen Family A8, MAGE-8 Antigen, MAGE8, Cancer/Testis Antigen 1.8, CT1.8, Cancer/Testis Antigen Family 1, Member 8, Cancer/Testis Antigen Family 1, Melanoma-Associated Antigen 8, Melanoma Antigen Family A, 8, Member 8, MAGEA8.
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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 MGSMLLGQKS QRYKAEEGLQ AQGEAPGLMD VQIPTAEEQK AASSSSTLIM GTLEEVTDSG SPSPPQSPEG ASSSLTVTDS TLWSQSDEGS SSNEEEGPST SPDPAHLESL FREALDEKVA ELVRFLLRKY QIKEPVTKAE MLESVIKNYK NHFPDIFSKA SECMQVIFGI DVKEVDPAGH SYILVTCLGL SYDGLLGDDQ STPKTGLLII VLGMILMEGS RAPEEAIWEA LSVMGLYDGR EHSVYWKLRK LLTQEWVQEN YLEYRQAPGS DPVRYEFLWG PRALAETSYV KVLEHVVRVN ARVRISYPSL HEEALGEEKG 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.
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Name :
HMGN1 HumanDescription:
High-Mobility Group Nucleosome Binding Domain 1 Human Recombinant
HMG14, GC104230, High-Mobility Group Nucleosome Binding Domain 1.
Product # :
PRO-821Price :
Quantity :
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Description
HMGN1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 108 amino acids (1-100 a.a.) and having a molecular mass of 11.7 kDa. HMGN1 protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
HMGN1 protein solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl, 0.1mM PMSF & 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
HMGN1 binds to the inner side of the nucleosomal DNA therefore changing the interaction between the DNA and the histone octamer. HMGN1 participates in the development which maintains transcribable genes in an exceptional chromatin conformation. HMGN1 inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2.
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Synonyms
HMG14, GC104230, High-Mobility Group Nucleosome Binding Domain 1.
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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
MPKRKVSSAE GAAKEEPKRR SARLSAKPPA KVEAKPKKAA AKDKSSDKKV QTKGKRGAKG KQAEVANQET KEDLPAENGE TKTEESPASD EAGEKEAKSD LEHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DKK3 Human, Sf9Description:
Dickkopf-Related Protein 3 Human Recombinant, Sf9
Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.
Product # :
PRO-2391Price :
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Description
DKK3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 338 amino acids (22-350a.a.) and having a molecular mass of 37.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).DKK3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
DKK3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Dickkopf-related protein 3 (DKK3) belongs to the DKK protein family including Dkk-1, 2, 3 and -4. DKK3 is a 350 amino acid secreted glycoprotein which is comprised of an N-terminal signal peptide and 2 conserved cysteine-rich domains that are separated by a 12 amino acid linker region. DKK3 is involved in embryonic development through its inhibition of the WNT signaling pathway. DKK3 gene expression is decreased in a variety of cancer cell lines and it may act as a tumor suppressor gene.
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Synonyms
Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.
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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
ADPAPAPTAT SAPVKPGPAL SYPQEEATLN EMFREVEELM EDTQHKLRSA VEEMEAEEAA AKASSEVNLA NLPPSYHNET NTDTKVGNNT IHVHREIHKI TNNQTGQMVF SETVITSVGD EEGRRSHECI IDEDCGPSMY CQFASFQYTC QPCRGQRMLC TRDSECCGDQ LCVWGHCTKM ATRGSNGTIC DNQRDCQPGL CCAFQRGLLF PVCTPLPVEG ELCHDPASRL LDLITWELEP DGALDRCPCA SGLLCQPHSH SLVYVCKPTF VGSRDQDGEI LLPREVPDEY EVGSFMEEVR QELEDLERSL TEEMALREPA AAAAALLGGE EIHHHHHH.
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 :
CKS1B HumanDescription:
CDC28 Protein Kinase Regulatory Subunit 1B Human Recombinant
CDC28 Protein Kinase Regulatory Subunit 1B, CDC28 Protein Kinase 1B, Cyclin-Dependent Kinases Regulatory Subunit 1, NB4 Apoptosis/Differentiation Related Protein, CDC2-Associated Protein CKS1, Cell Division Control Protein CKS1, CDC28 Protein Kinase 1, PNAS-143, PNAS-16, PNAS-18, CKS-1, ckshs1.
Product # :
PRO-1834Price :
Quantity :
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Description
CKS1B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (1-79) and having a molecular mass of 12.0 kDa. CKS1B is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The CKS1B solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
CKS1B protein which binds to the catalytic subunit of cyclin dependent kinases is vital for their biological function. The CKS1B mRNA is expressed in HeLa cells during the course of cell cycle in several forms which suggests that the encoded protein has a particular function. Two transcript variants were identified for this gene however it seems that only one of them encodes a protein.
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Synonyms
CDC28 Protein Kinase Regulatory Subunit 1B, CDC28 Protein Kinase 1B, Cyclin-Dependent Kinases Regulatory Subunit 1, NB4 Apoptosis/Differentiation Related Protein, CDC2-Associated Protein CKS1, Cell Division Control Protein CKS1, CDC28 Protein Kinase 1, PNAS-143, PNAS-16, PNAS-18, CKS-1, ckshs1.
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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 MGSMSHKQIY YSDKYDDEEF EYRHVMLPKD IAKLVPKTHL MSESEWRNLG VQQSQGWVHY MIHEPEPHIL LFRRPLPKKP KK
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 :
CUTA HumanDescription:
CutA Divalent Cation Tolerance Homolog Human Recombinant
ACHAP, C6orf82, MGC111154, cutA divalent cation tolerance homolog, CUTA.
Product # :
PRO-812Price :
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Description
CUTA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids (33-179 a.a.) and having a molecular mass of 17.1 kDa. CUTA protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
CUTA Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
CUTA is the 179 amino acid mammalian homolog of the cutA E. coli protein and is ubiquitously expressed, particularly in brain tissue. CUTA participates in cellular tolerance to a broad range of divalent cations other than copper. The CUTA protein is a cytoplasmic protein, encoded by the single-gene operon and has been related to divalent cation tolerance.
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Synonyms
ACHAP, C6orf82, MGC111154, cutA divalent cation tolerance homolog, CUTA.
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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
MRLLLLPRVL LTMASGSPPT QPSPASDSGS GYVPGSVSAA FVTCPNEKVA KEIARAVVEK RLAACVNLIP QITSIYEWKG KIEEDSEVLM MIKTQSSLVP ALTDFVRSVH PYEVAEVIAL PVEQGNFPYL QWVRQVTESV SDSITVLPLE 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 :
VEGI HumanDescription:
Human Vascular Endothelial Growth Inhibitor Recombinant
Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.
Product # :
CYT-517Price :
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Shipped at Room temp
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Description
TNFSF15 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 20.5kDa. The TNFSF15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TNFSF15 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4 with 0.02% Tween-20.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by its ability to induce apoptosis using human TF-1 cells is less than 20ng/ml, corresponding to a specific activity of > 5.0×104 IU/mg.More Info
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Introduction
TNFSF15 is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein is abundantly expressed in endothelial cells, but is not expressed in either B or T cells. The expression of TNFSF15 is inducible by TNF and IL-1 alpha. This cytokine is a ligand for receptor TNFRSF25 and decoy receptor TNFRSF21/DR6. It can activate NF-kappaB and MAP kinases, and acts as an autocrine factor to induce apoptosis in endothelial cells. TNFSF15 is also found to inhibit endothelial cell proliferation, and thus may function as an angiogenesis inhibitor. An additional isoform encoded by an alternatively spliced transcript variant has been reported but the sequence of this transcript has not been determined.
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Synonyms
Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
TNFSF15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGI 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 TNFSF15 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
MQLTKGRLHFSHPLSHTKHISPFVTDAPLRADGDKPRAHL
TVVRQTPTQHFKNQFPALHWEHELGLAFTKNRMNYTNKF
LLIPESGDYFIYSQVTFRGMTSECSEIRQAGRPNKPDSIT
VVITKVTDSYPEPTQLLMGTKSVCEVGSNWFQPIYLGAM
FSLQEGDKLMVNVSDISLVDYTKEDKTFFGAFLL.
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 :
RBP4 ProteinDescription:
Retinol Binding Protein-4 Human
Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.
Product # :
CYT-1218Price :
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Shipped at Room temp
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Description
RBP4 Human produced in Pooled human plasma can be used as a calibrator in immunoassays. Immunoreactivity was checked using monoclonal antibodies specific to RBP4.
Source
Human Plasma.
Formulation
RBP4 was lyophilized from PBS, 150mM NaCl, and 10mM K-phosphate, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Retinol Binding Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RBP4 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 RBP4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Retinol Binding Protein 4 (RBP4) is a multifunctional protein that plays a crucial role in the transport of retinol (vitamin A) in the bloodstream. Beyond its traditional role in vitamin A metabolism, RBP4 has emerged as a key player in various physiological processes and pathological conditions. This research endeavors to explore the diverse facets of RBP4 in human biology, shedding light on its physiological functions, regulatory mechanisms, and implications in health and disease.
Physiological Functions:
At its core, RBP4 acts as a carrier protein, shuttling retinol from the liver, where it is stored, to peripheral tissues where it is utilized. Retinol is vital for vision, immune function, growth, and development, making RBP4 an essential component in these processes. By regulating the availability of retinol, RBP4 contributes significantly to maintaining normal vision, immune responses, and cellular differentiation, particularly in epithelial tissues.
Metabolic Significance:
Research has unveiled RBP4’s role in metabolic regulation. It has been associated with insulin resistance, a hallmark of type 2 diabetes mellitus. Elevated RBP4 levels are observed in individuals with obesity and insulin resistance, implicating its involvement in metabolic disorders. Understanding the interplay between RBP4, insulin signaling, and glucose metabolism is crucial for deciphering the complexities of diabetes and metabolic syndrome.
Immunological Implications:
Beyond its metabolic functions, RBP4 has been implicated in immune responses. Studies have suggested its involvement in modulating inflammatory processes and immune cell functions. By influencing immune cell differentiation and cytokine production, RBP4 may play a role in both immune defense and autoimmune disorders. Investigating these immunological implications provides insights into the crosstalk between metabolic and immune pathways.
Genetic and Environmental Influences:
Genetic variations and environmental factors, such as diet and lifestyle, can impact RBP4 levels and functions. Research into these influences is essential for understanding individual susceptibility to metabolic disorders and inflammatory conditions. Genetic studies shed light on the hereditary aspects of RBP4 regulation, providing valuable information for personalized medicine approaches.
Clinical Relevance:
RBP4’s involvement in various diseases, including diabetes, cardiovascular diseases, and certain cancers, underscores its clinical relevance. It serves as a potential biomarker for metabolic dysregulation and a target for therapeutic interventions. Moreover, RBP4-targeted therapies are being explored for their potential in managing metabolic disorders and related complications.
Conclusion:
RBP4, once primarily recognized for its role in vitamin A transport, has evolved into a multifaceted protein with intricate roles in metabolism, immunity, and disease. Its functions extend far beyond being a mere carrier of retinol, influencing diverse physiological processes and serving as a nexus between metabolic health and immunological responses. Unraveling the complexities of RBP4 opens avenues for understanding diseases like diabetes and offers promising prospects for innovative therapies, emphasizing its significance in human biology and medicine.
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 :
PDCL HumanDescription:
Phosducin-Like Human Recombinant
Phosducin-like protein, PHLP, DKFZp564M1863.
Product # :
PRO-1141Price :
Quantity :
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Description
PDCL Human Recombinant produced in E. coli is a single polypeptide chain containing 325 amino acids (1-301) and having a molecular mass of 36.8 kDa.PDCL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PDCL solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Phosducin-like protein (PDCL) is a member of the phosducin family. PDCL is a putative modulator of heterotrimeric G proteins. PDCL shares broad amino acid sequence homology with phosducin, a phosphoprotein expressed in the retina and pineal gland. Both PDCL and phosphoducin regulate G-protein signaling by binding to the beta-gamma subunits of G proteins.
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Synonyms
Phosducin-like protein, PHLP, DKFZp564M1863.
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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 MGSHMTTLDD KLLGEKLQYY YSSSEDEDSD HEDKDRGRCA PASSSVPAEA ELAGEGISVN TGPKGVINDW RRFKQLETEQ REEQCREMER LIKKLSMTCR SHLDEEEEQQ KQKDLQEKIS GKMTLKEFAI MNEDQDDEEF LQQYRKQRME EMRQQLHKGP QFKQVFEISS GEGFLDMIDK EQKSIVIMVH IYEDGIPGTE AMNGCMICLA AEYPAVKFCK VKSSVIGASS QFTRNALPAL LIYKGGELIG NFVRVTDQLG DDFFAVDLEA FLQEFGLLPE KEVLVLTSVR NSATCHSEDS DLEID
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 :
Protein A, 434 a.aDescription:
Staphylococcal Protein A 434 a.a Recombinant
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-686Price :
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Description
Recombinant Staphylococcal Protein A produced in E.Coli is a non-glycosylated, Polypeptide chain containing 434 amino acids (37-469 a.a.) and having a molecular mass of 48.1 kDa. Recombinant Staphylococcal Protein A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Protein-A protein solution contains 20mM Tris-HCl, pH-8 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Protein A is a cell wall protein deriving from Staphylococcus aureus which exhibits unique binding properties for IgG from a variety of mammalian species and for some IgM and IgA as well. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. It couples to a wide variety of reporter molecules including fluorescent dyes, enzyme markers, biotin, colloidal gold and radioactive iodine without affecting the antibody binding site. Recombinant Protein A was developed to increase the specificity of the molecule for IgG and is widely used both in research and bioprocessing. The recombinant protein A is produced by expressing a modified protein A gene in E.coli. A specific purification process with strict quality control was taken to get the recombinant protein A with the purity of more than 98% , no human IgG affinity step is used during validated fermentation and purification and devoid of bacterial contaminant found normally in native Protein A. (Free of Staphylococcus endotoxins and hemolysin).
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Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
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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
MAQHDEAQQN AFYQVLNMPN LNADQRNGFI QSLKDDPSQS ANVLGEAQKL NDSQAPKADA QQNNFNKDQQ SAFYEILNMP NLNEAQRNGFIQSLKDDPSQ STNVLGEAKK LNESQAPKAD NNFNKEQQNA FYEILNMPNL NEEQRNGFIQ SLKDDPSQSA NLLSEAKKLN ESQAPKADNK
FNKEQQNAFY EILHLPNLNE EQRNGFIQSL KDDPSQSANL LAEAKKLNDA QAPKADNKFN KEQQNAFYEI LHLPNLTEEQ RNGFIQSLKDDPSVSKEILA EAKKLNDAQA PKEEDNNKPG KEDNNKPGKE DNNKPGKEDG NKPGKEDNKK PGKEDNKKPG KEDNKKPGKE DGNKPGKEDN
KKPGKEDGNG VHVVKPGDTV NDIAKANGTT ADKIAADNKL ADKNMIKPGQ ELVVDKKQPA NHADANKAQA LPET.
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 :
DTL HumanDescription:
Denticleless E3 Ubiquitin Protein Ligase Human Recombinant
L2DTL, DCAF2, RAMP, CDT2.
Product # :
PRO-2826Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The DTL Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The DTL His-Tagged Fusion Protein, produced in E. coli, is a 31kDa protein containing 126 amino acid residues of the DTL Human, 1-231 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
L2DTL, DCAF2, RAMP, CDT2.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized DTL 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 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
Denticleless E3 ubiquitin protein ligase (DTL) is part of the E3 ubiquitin ligase family, fundamental to the ubiquitin-proteasome system, which adjusts protein degradation and modification in cells. DTL also participates in numerous critical biological processes, which comprises cell cycle progression, DNA repair, as well as embryonic development. More than a few diseases have been linked with the dysregulation of DTL in particular Cancer, this highlights the importance of DTL as a potential therapeutic goal. DTL takes an important part in regulating the cell cycle, mainly the transition from the G1 phase to the S phase. The degradation of cell cycle regulators, such as cyclins, is also mediated by DTL in that way assuring appropriate cell division in addition to preventing uncontrolled proliferation. DTL is also part of the DNA damage response mechanisms. It ubiquitinates vital proteins which are involved in DNA repair pathways, thus influencing the cellular response to genotoxic stress and preserving genomic integrity.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IFNAR1 HumanDescription:
Interferon Alpha and Beta Receptor Subunit 1 Human Recombinant
IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 1.
Product # :
CYT-1138Price :
Quantity :
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Shipped with Ice Packs
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- SDS-PAGE
Description
IFNAR1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 415 amino acids (28-436a.a.) and having a molecular mass of 47.9kDa. IFNAR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
IFNAR1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
Interferon Alpha And Beta Receptor or IFNAR1, is part of the class II cytokine receptor family. IFNAR1 forms one of the two chains of a receptor for interferons alpha and beta. IFNAR1 binds and activates the receptor that stimulates Janus protein kinases, which then phosphorylate few proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also acts as an antiviral factor.
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Synonyms
IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 1.
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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
KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.
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Background
What is the molecular weight/Mw of IFNAR1 HUMAN Protein?
IFNAR1 HUMAN Protein has a total Mw of 47.9kDa.
What is the source or expression system of IFNAR1 HUMAN Protein?
Sf9, Insect cells.
What is the Purity of IFNAR1 HUMAN Protein?
IFNAR1 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNAR1 HUMAN Protein?
The biological functionality of IFNAR1 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IFNAR1 HUMAN Protein?
KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.
What applications can IFNAR1 HUMAN Protein be used in?
IFNAR1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNAR1 HUMAN Protein?
The endotoxin level is minimal, IFNAR1 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.
- View Data Sheet
Name :
HSBP1L1 HumanDescription:
Heat Shock Factor Binding Protein 1-Like 1 Human Recombinant
Heat shock factor-binding protein 1-like protein 1, HSBP1L1, Heat Shock Factor Binding Protein 1-Like 1, Heat shock factor binding protein 1-like.
Product # :
HSP-063Price :
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Shipping Method :
Shipped with Ice Packs
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Description
HSBP1L1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (1-74 a.a) and having a molecular mass of 10.8kDa.HSBP1L1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HSBP1L1 protein solution (1mg/ml) containing Phosphate buffer saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Heat Shock Factor Binding Protein 1-Like 1 (HSBP1L1) is a part of a family of eukaryotic proteins known as nucleotide exchange factors for HSP 70. HSBP1L1 is a protein coding gene whose expression is regulated mainly at the transcription level.
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Synonyms
Heat shock factor-binding protein 1-like protein 1, HSBP1L1, Heat Shock Factor Binding Protein 1-Like 1, Heat shock factor binding protein 1-like.
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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 MGSMDVRGPE APGGRALRDA AENLFQELQE HFQALTATLN LRMEEMGNRI EDLQKNVNDL MVQAGIENSI KEQMLKT.
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 :
TIMM8A HumanDescription:
Translocase of Inner Mitochondrial Membrane 8 Homolog A Human Recombinant
Mitochondrial import inner membrane translocase subunit Tim8 A, TIMM8A, Translocase of Inner Mitochondrial Membrane 8 Homolog A, DDP, DDP1, DFN1, MTS, TIM8, Deafness dystonia protein 1, X-linked deafness dystonia protein.
Product # :
PRO-1818Price :
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Description
TIMM8A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (1-97) and having a molecular mass of 13.4 kDa.TIMM8A is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TIMM8A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Translocase of Inner Mitochondrial Membrane 8 Homolog A (TIMM8A) takes part in the import and insertion of hydrophobic membrane proteins from the cytoplasm into the mitochondrial. TIMM8A plays a role as a chaperone-like protein which protects the hydrophobic precursors from aggregation and leads them through the mitochondrial intermembrane space. TIMM8A is essential for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Defects in TIMM8A cause Jensen syndrome. TIMM8A and TIMM13, forms a 70 kDa heterohexamer.
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Synonyms
Mitochondrial import inner membrane translocase subunit Tim8 A, TIMM8A, Translocase of Inner Mitochondrial Membrane 8 Homolog A, DDP, DDP1, DFN1, MTS, TIM8, Deafness dystonia protein 1, X-linked deafness dystonia 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
MGSSHHHHHH SSGLVPRGSH MGSMDSSSSS SAAGLGAVDP QLQHFIEVET QKQRFQQLVH QMTELCWEKC MDKPGPKLDS RAEACFVNCV ERFIDTSQFI LNRLEQTQKS KPVFSESLSD.
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 :
ARL1 HumanDescription:
ADP-Ribosylation Factor-Like 1 Human Recombinant
ARFL1.
Product # :
PRO-508Price :
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Shipping Method :
Shipped with Ice Packs
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Description
ARL1 Recombinant Human 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 22.5 kDa. The ARL1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARL1 solution (0.25mg/ml) containing 20mM Tris-HCl pH-8, 2mM DTT, 100mM NaCl and 40% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ARL1 is part of the ARL (ADP-ribosylation factor-like) family of proteins, which are structurally associated to ADP-ribosylation factors (ARFs). ARFs, described as activators of cholera toxin (CT) ADP-ribosyltransferase activity, control intracellular vesicular membrane trafficking, and stimulate a phospholipase D (PLD) isoform.
ARL1 is a weak stimulator of PLD and CT in a phospholipid dependent manner.
ARL1 is a GTP-binding protein that has low efficiency as allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. ARL1 is involved in the Golgi apparatus. -
Synonyms
ARFL1.
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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 MGGFFSSIFS SLFGTREMRI LILGLDGAGK TTILYRLQVG EVVTTIPTIG FNVETVTYKN LKFQVWDLGG QTSIRPYWRC YYSNTDAVIY VVDSCDRDRI GISKSELVAM LEEEELRKAI LVVFANKQDM EQAMTSSEMA NSLGLPALKD RKWQIFKTSA TKGTGLDEAM EWLVETLKSR 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.
- View Data Sheet
Name :
EDA2R HumanDescription:
Ectodysplasin A2 Receptor Human Recombinant
Ectodysplasin A2 Receptor, XEDAR, TNFRSF27, EDA-A2 Receptor, X-Linked Ectodysplasin-A2 Receptor, EDAA2R, EDA-A2R, Tumor Necrosis Factor Receptor Superfamily Member 27, Tumor Necrosis Factor Receptor Superfamily Member XEDAR, EDAR2.
Product # :
PRO-1744Price :
Quantity :
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Shipped with Ice Packs
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Description
EDA2R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (1-138 a.a) and having a molecular mass of 17.7kDa.EDA2R is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EDA2R protein solution (1mg/ml) containing 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
EDA2R (ectodysplasin A2 receptor) mediates the activation of the NF-kappa-B and JNK pathways. Activation seems to be mediated through binding to TRAF3 and TRAF6. In addition, Mutations in EDA give rise to a clinical syndrome characterized by loss of hair, sweat glands, and teeth. EDA2R specifically binds to EDA-A2 isoform. This protein is a type III transmembrane protein of the TNFR (tumor necrosis factor receptor) superfamily, and contains 3 cysteine-rich repeats and a single transmembrane domain however it lacks an N-terminal signal peptide. Alternatively spliced transcript variants have been found for this gene. Among the diseases associated with EDA2R are ectodermal dysplasia 1, hypohidrotic, x-linked, and hypohidrotic ectodermal dysplasia.
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Synonyms
Ectodysplasin A2 Receptor, XEDAR, TNFRSF27, EDA-A2 Receptor, X-Linked Ectodysplasin-A2 Receptor, EDAA2R, EDA-A2R, Tumor Necrosis Factor Receptor Superfamily Member 27, Tumor Necrosis Factor Receptor Superfamily Member XEDAR, EDAR2.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDCQENE YWDQWGRCVT CQRCGPGQEL SKDCGYGEGG DAYCTACPPR RYKSSWGHHR CQSCITCAVI NRVQKVNCTA TSNAVCGDCL PRFYRKTRIG GLQDQECIPC TKQTPTSEVQ CAFQLSLVEA DAPTVPPQEA T
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 :
RNF7 HumanDescription:
Ring Finger Protein 7 Human Recombinant
RING-box protein 2 isoform 1, Ring finger protein 7, CKBBP1, ROC2, SAG, RING-box protein 2, Rbx2, CKII beta-binding protein 1, Regulator of cullins 2, Sensitive to apoptosis gene protein, RBX2, RNF7.
Product # :
PRO-1671Price :
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Shipped with Ice Packs
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Description
RNF7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (1-113 a.a) and having a molecular mass of 15.1kDa.RNF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RNF7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ring Finger Protein 7, also known as RNF7, is an extremely conserved ring finger protein. RNF7 is a vital subunit of SKP1-cullin/CDC53-F box protein ubiquitin ligases that are a part of the protein degradation machinery important for cell cycle progression and signal transduction. RNF7 is a substrate of casein kinase II (CSNK2A1/CKII) and also interacts with it. The phosphorylation of RNF7 by CSNK2A1 promotes the degradation of IkappaBalpha (CHUK/IKK-alpha/IKBKA) and p27Kip1(CDKN1B).
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Synonyms
RING-box protein 2 isoform 1, Ring finger protein 7, CKBBP1, ROC2, SAG, RING-box protein 2, Rbx2, CKII beta-binding protein 1, Regulator of cullins 2, Sensitive to apoptosis gene protein, RBX2, RNF7.
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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 MGSMADVEDG EETCALASHS GSSGSKSGGD KMFSLKKWNA VAMWSWDVEC DTCAICRVQV MDACLRCQAE NKQEDCVVVW GECNHSFHNC CMSLWVKQNN RCPLCQQDWV VQRIGK.
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 :
BID Mouse, GSTDescription:
BH3 Interacting Domain Death Agonist Mouse Recombinant, GST
BH3-interacting domain death agonist, p22 BID, BID, FP497, MGC15319, MGC42355.
Product # :
PRO-643Price :
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Description
BID Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 1-195 amino acids and having a molecular mass of 48 kDa.The Mouse BID is expressed as GST-Tag fusion protein and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
The Mouse GST tag BID protein solution contains 10mM Tris-HCl pH-8, 1mM EDTA and 250mM NaCl.
Purity
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
BID is a pro-apoptotic Bcl-2 protein having only the BH3 domain. In reaction to apoptotic signaling, BID interacts with another Bcl-2 family of cell death regulators, called Bax, they form a heterodimer resulting to the insertion of Bax into the outer mitochondrial membrane. Bax induces the opening of the mitochondrial voltage-dependent anion channel which lead to the release of cytochrome c and other pro-apoptotic factors from the mitochondria resulting in activation of caspases. BID is a mediator of mitochondrial damage induced by caspase-8 (CASP8). CASP8 cleaves BID, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. The major proteolytic product p15 BID releasea cytochrome c. Isoform 1, Isoform 2 and Isoform 4 induce ice-like proteases and apoptosis while Isoform 3 does not induce apoptosis.
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Synonyms
BH3-interacting domain death agonist, p22 BID, BID, FP497, MGC15319, MGC42355.
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Physical Appearance
Sterile Filtered colorless 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.
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 :
D-Dimer HumanDescription:
D-Dimer Human
Product # :
PRO-2795Price :
Quantity :
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Shipped at Room temp
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Description
D-Dimer Human produced in Human Plasma is a specific degradation product of cross-linked fibrin and is used as a marker of hypercoagulation state that causes cardio-vascular diseases. D-Dimer is purified by proprietary chromatographic technique.
Source
Human plasma.
Formulation
D-Dimer was lyophilized from 10mM Tris-HCl and 0.15M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized D-Dimer although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution D-Dimer 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 D-Dimer in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
D-dimer, a small protein fragment present in the blood after a blood clot dissolves, is a vital marker in the realms of hematology and vascular medicine. Its presence signifies the ongoing process of fibrinolysis, where clots formed in blood vessels are broken down. Beyond its diagnostic significance, understanding the roles of D-dimer in human physiology and pathology is essential for comprehending coagulation disorders and cardiovascular diseases. This research delves into the multifaceted aspects of D-dimer, exploring its physiological functions, diagnostic applications, and implications in various medical conditions.
Physiological Functions:
In physiological conditions, coagulation and fibrinolysis are finely regulated processes, ensuring hemostasis and preventing excessive bleeding or clot formation. D-dimer is a natural byproduct of fibrinolysis, created when plasmin, an enzyme, breaks down fibrin clots. In this context, D-dimer acts as a marker of the body's intricate balance between clot formation and dissolution. It reflects the ongoing maintenance of vascular integrity, showcasing the body's ability to prevent unnecessary clotting.
Diagnostic Significance:
D-dimer holds significant diagnostic value, especially in the context of thrombotic disorders. Elevated levels of D-dimer in the blood are indicative of increased fibrinolysis, potentially signaling an underlying clotting disorder. Clinically, D-dimer assays are widely used to rule out thromboembolic events, such as deep vein thrombosis (DVT) or pulmonary embolism (PE). Moreover, D-dimer levels are crucial in risk stratification and decision-making processes in emergency departments, aiding in the timely diagnosis and treatment of thrombotic conditions.
Cardiovascular Implications:
Research has indicated a strong correlation between elevated D-dimer levels and cardiovascular diseases. In conditions like coronary artery disease (CAD) and stroke, where abnormal clot formation contributes to pathogenesis, D-dimer serves as a prognostic marker. Its presence hints at the ongoing vascular damage and the potential risk of acute events. Studying these correlations provides valuable insights into the progression of cardiovascular diseases, aiding in the development of targeted therapeutic strategies.
Beyond Coagulation Disorders:
Interestingly, recent research has begun to explore D-dimer's involvement in conditions beyond coagulation disorders. Studies suggest links between elevated D-dimer levels and inflammatory diseases, such as sepsis and rheumatoid arthritis. This expanding scope highlights the intricate interplay between coagulation, inflammation, and immune responses, shedding light on novel avenues for therapeutic interventions.
Conclusion:
D-dimer, once a simple marker of fibrinolysis, has evolved into a multifaceted indicator in the realm of medicine. Its physiological role as a byproduct of clot dissolution is intertwined with its diagnostic significance in thrombotic events and cardiovascular diseases. Furthermore, emerging research is uncovering its involvement in inflammatory processes, broadening its clinical implications. By delving into the complexities of D-dimer, scientists and clinicians pave the way for a deeper understanding of coagulation disorders and associated conditions, driving advancements in diagnostics and therapies.
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 :
CHMP6 HumanDescription:
Charged Multivesicular Body Protein 6 Human Recombinant
Charged multivesicular body protein 6, Chromatin-modifying protein 6, Vacuolar protein sorting-associated protein 20, Vps20, hVps20, CHMP6.
Product # :
PRO-1085Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CHMP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-201 a.a) and having a molecular mass of 26.1kDa (Molecular size on SDS-PAGE will appear higher).CHMP6 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CHMP6 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Charged multivesicular body protein 6 (CHMP6) is a member of the SNF7 family. The CHMP6 protein is a core component of the endosomal sorting necessary for transport complex III (ESCRT-III) that is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) which are produced by invagination and scission from the limiting membrane of the endosome and generally are transported to lysosomes facilitating degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids.
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Synonyms
Charged multivesicular body protein 6, Chromatin-modifying protein 6, Vacuolar protein sorting-associated protein 20, Vps20, hVps20, CHMP6.
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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 MGSHMGNLFG RKKQSRVTEQ DKAILQLKQQ RDKLRQYQKR IAQQLERERA LARQLLRDGR KERAKLLLKK KRYQEQLLDR TENQISSLEA MVQSIEFTQI EMKVMEGLQF GNECLNKMHQ VMSIEEVERI LDETQEAVEY QRQIDELLAG SFTQEDEDAI LEELSAITQE QIELPEVPSE PLPEKIPENV PVKARPRQAE LVAAS.
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 :
Ag85ADescription:
Mycobacterium Tuberculosis major secretory protein Antigen 85A Recombinant
Ronectin-binding protein A, Mycolyl transferase 85A.
Product # :
PRO-1076Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
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Description
Recombinant Mycobacterium tuberculosis Ag85A (43-338 a.a) produced in Hi-5 cells is a single, glycosylated polypeptide chain having a molecular mass of 32.8kDa (305 a.a in total).Antigen 85A is fused to a 6 amino acid His tag at C-terminus and purified by conventional chromatographic techniques.
Source
Baculovirus
Formulation
The Ag85A solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Antigen 85A is a member of the antigen 85 complex (Antigen 85A, B, C). The enzymes of the antigen 85 complex have mycolyltransferase activity and catalyze the synthesis of the very rich glycolipid of the mycobacterial cell wall, the cord factor (trehalose 6,6'-dimycolate, TDM). The cord factor is vital for the integrity of the mycobacterial cell wall and pathogenesis of the bacillus. TDM is synthesized from two molecules of trehalose-6'-monomycolate (TMM) by Antigen 85A.
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Synonyms
Ronectin-binding protein A, Mycolyl transferase 85A.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPAFSRPGL PVEYLQVPSP SMGRDIKVQF QSGGANSPAL YLLDGLRAQD DFSGWDINTP AFEWYDQSGL SVVMPVGGQS SFYSDWYQPA CGKAGCQTYK WETFLTSELP GWLQANRHVK PTGSAVVGLS MAASSALTLA IYHPQQFVYA GAMSGLLDPS QAMGPTLIGL AMGDAGGYKA SDMWGPKEDP AWQRNDPLLN VGKLIANNTR VWVYCGNGKP SDLGGNNLPA KFLEGFVRTS NIKFQDAYNA GGGHNGVFDF PDSGTHSWEY WGAQLNAMKP DLQRALGATP NTGPAPQGAH HHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
A2LD1 HumanDescription:
AIG2-Like Domain 1 Human Recombinant
Gamma-glutamylaminecyclotransferase, GGACT, AIG2-like domain-containing protein 1, A2LD1.
Product # :
PRO-172Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
A2LD1 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 173 amino acids (1-153 a.a.) and having a molecular mass of 19.4kDa. The A2LD1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The A2LD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Gamma-glutamylaminecyclotransferase (A2LD1) is an enzyme which converts gamma-glutamylamines to free amines and 5-oxoproline. A2LD1 demonstrates high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. A2LD1 assists in the proteolytic degradation of crosslinked fibrin by breaking down isodipeptide L-gamma-glutamyl-L-epsilon-lysine, which is a byproduct of fibrin degradation. The reaction catalyzed by the A2LD1 produces 5-oxo-L-proline and a free alkylamine.
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Synonyms
Gamma-glutamylaminecyclotransferase, GGACT, AIG2-like domain-containing protein 1, A2LD1.
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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 MALVFVYGTL KRGQPNHRVL RDGAHGSAAF RARGRTLEPY PLVIAGEHNI PWLLHLPGSG RLVEGEVYAV DERMLRFLDD FESCPALYQR TVLRVQLLED RAPGAEEPPA PTAVQCFVYS RATFPPEWAQ LPHHDSYDSE GPHGLRYNPR ENR.
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 :
MAPT HumanDescription:
Microtubule-Associated Protein Tau Human Recombinant
TAU, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, PPND.
Product # :
PRO-295Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MAPT Recombinant Human (Isoform-4) produced in E.Coli is a single, non-glycosylated polypeptide chain containing 372 amino acids (1-352 a.a.) and having a molecular mass of 38.9 kDa (Real molecular weight on SDS-PAGE will be shift up). The MAPT is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAPT solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT, 0.2M NaCl & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
MAPT is a neuronal microtubule associated protein localized mostly on axons.
MAPT promotes tubulin polymerisation and stabilizes microtubules, however it also serves to connect certain signalling pathways to the cytoskeleton. MAPT, in its hyperphosphorylated form, is the main part of paired helical filaments (PHF) and neurofibrillary lesions in Alzheimer''s disease (AD) brain. -
Synonyms
TAU, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, PPND.
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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 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQIV YKPVDLSKVT SKCGSLGNIH HKPGGGQVEV KSEKLDFKDR VQSKIGSLDN ITHVPGGGNK KIETHKLTFR ENAKAKTDHG AEIVYKSPVV SGDTSPRHLS NVSSTGSIDM VDSPQLATLA DEVSASLAKQ GL.
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.