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1000 results found for “Cysteine-Rich Secretory Protein”
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Name :
PSTPIP1 HumanDescription:
Proline-Serine-Threonine Phosphatase Interacting Protein 1 Human Recombinant
Proline-serine-threonine phosphatase interacting protein 1, CD2BP1, CD2BP1L, CD2BP1S, H-PIP, PAPAS, PSTPIP, PSTPIP1, Proline-serine-threonine phosphatase-interacting protein 1, PEST phosphatase-interacting protein 1, CD2-binding protein 1.
Product # :
PRO-1515Price :
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Description
PSTPIP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (1-416) and having a molecular mass of 50 kDa.PSTPIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PSTPIP1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Proline-Serine-Threonine Phosphatase Interacting Protein 1 (PSTPIP1) which is a scaffold protein and a regulator of the actin cytoskeleton binds ABL1, PTPN18, WAS, CD2AP, and PTPN12. PSTPIP1 also binds to the cytoplasmic tail of CD2, an effector of T cell activation and adhesion, negatively affecting CD2-triggered T cell activation. Mutations in PSTPIP1 are a cause of PAPA syndrome.
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Synonyms
Proline-serine-threonine phosphatase interacting protein 1, CD2BP1, CD2BP1L, CD2BP1S, H-PIP, PAPAS, PSTPIP, PSTPIP1, Proline-serine-threonine phosphatase-interacting protein 1, PEST phosphatase-interacting protein 1, CD2-binding protein 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
MGSSHHHHHH SSGLVPRGSH MGSMMPQLQF KDAFWCRDFT AHTGYEVLLQ RLLDGRKMCK DMEELLRQRA QAEERYGKEL VQIARKAGGQ TEINSLRASF DSLKQQMENV GSSHIQLALT LREELRSLEE FRERQKEQRK KYEAVMDRVQ KSKLSLYKKA MESKKTYEQK CRDADDAEQA FERISANGHQ KQVEKSQNKA RQCKDSATEA ERVYRQSIAQ LEKVRAEWEQ EHRTTCEAFQ LQEFDRLTIL RNALWVHSNQ LSMQCVKDDE LYEEVRLTLE GCSIDADIDS FIQAKSTGTE PPAPVPYQNY YDREVTPLTS SPGIQPSCGM IKRFSGLLHG SPKTTSLAAS AASTETLTPT PERNEGVYTA IAVQEIQGNP ASPAQEYRAL YDYTAQNPDE LDLSAGDILE VILEGEDGWW TVERNGQRGF VPGSYLEKL.
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 :
CLNS1A HumanDescription:
Chloride Channel, Nucleotide-Sensitive, 1A Human Recombinant
CLNS1A, CLCI, ICLN, CLNS1B, Methylosome subunit pICln, Chloride channel, nucleotide sensitive 1A, Chloride conductance regulatory protein ICln, Chloride ion current inducer protein, Reticulocyte pICln.
Product # :
PRO-1277Price :
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Description
CLNS1A Human Recombinant produced in E. coli is a single polypeptide chain containing 261 amino acids (1-237) and having a molecular mass of 28.8kDa (molecular size on SDS-PAGE will appear higher).CLNS1A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CLNS1A solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Methylosome subunit pICln (CLNS1A), is a member of the pICln (TC 1.A.47) family. CLNS1A takes part in multiple regulatory pathways. CLNS1A interaction with Sm proteins, inhibits their compilation on U RNA and interferes with snRNP biogenesis. CLNS1A inhibits the binding of survival motor neuron protein (SMN) to Sm proteins. Methylosome subunit pICln is related with the plasma membrane where it functions as a chloride present regulator.
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Synonyms
CLNS1A, CLCI, ICLN, CLNS1B, Methylosome subunit pICln, Chloride channel, nucleotide sensitive 1A, Chloride conductance regulatory protein ICln, Chloride ion current inducer protein, Reticulocyte pICln.
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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 MGSHMSFLKS FPPPGPAEGL LRQQPDTEAV LNGKGLGTGT LYIAESRLSW LDGSGLGFSL EYPTISLHAL SRDRSDCLGE HLYVMVNAKF EEESKEPVAD EEEEDSDDDV EPITEFRFVP SDKSALEAMF TAMCECQALH PDPEDEDSDD YDGEEYDVEA HEQGQGDIPT FYTYEEGLSH LTAEGQATLE RLEGMLSQSV SSQYNMAGVR TEDSIRDYED GMEVDTTPTV AGQFEDADVD H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NHEJ1 HumanDescription:
Nonhomologous End-Joining Factor 1 Human Recombinant
Nonhomologous end-joining factor 1, Protein cernunnos, XRCC4-like factor, Cernunnos, XLF, FLJ12610.
Product # :
PRO-1193Price :
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Description
NHEJ1 Human Recombinant produced in E. coli is a single polypeptide chain containing 247 amino acids (1-224) and having a molecular mass of 27.8 kDa.NHEJ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NHEJ1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Non-homologous end-joining factor 1 (NHEJ1) is a member of the XLF family. NHEJ1 is a DNA repair factor vital for the nonhomologous end-joining pathway, which preferentially mediates repair of double-stranded breaks. NHEJ1 gene mutations cause different kinds of severe combined immunodeficiency disorders. NHEJ1 was initially detected as the protein mutated in five patients with growth retardation, microcephaly, and immunodeficiency. In addition, patients with NHEJ1 mutations have immunodeficiency caused by a defect in V(D)J recombination, which employs NHEJ to promote immune system diversity.
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Synonyms
Nonhomologous end-joining factor 1, Protein cernunnos, XRCC4-like factor, Cernunnos, XLF, FLJ12610.
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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 MGS MEELEQG LLMQPWAWLQ LAENSLLAKV FITKQGYALL VSDLQQVWHE QVDTSVVSQR AKELNKRLTA PPAAFLCHLD NLLRPLLKDA AHPSEATFSC DCVADALILR VRSELSGLPF YWNFHCMLAS PSLVSQHLIR PLMGMSLALQ CQVRELATLL HMKDLEIQDY QESGATLIRD RLKTEPFEEN SFLEQFMIEK LPEACSIGDG KPFVMNLQDL YMAVTTQ
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 :
PDCD1 Human, ActiveDescription:
Programmed Cell Death 1 Human Recombinant, Active
Programmed cell death protein 1, CD279, hPD-1, SLEB2, hPD-l, hSLE1, PD-1, PD1, PDCD1.
Product # :
PRO-2724Price :
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Description
PDCD1 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 383 amino acids (21-170 a.a) and having a molecular mass of 42.9kDa.PDCD1 is fused to a 233 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The PDCD1 solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with Human PD-L1/B7-H1
More Info
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Introduction
PDCD1 is a cell surface membrane protein of the immunoglobulin superfamily. PDCD1 is expressed in pro-B-cells and is thought to have a role in their differentiation. In mice, expression of PDCD1 gene is induced in the thymus when anti-CD3 antibodies are injected and large numbers of thymocytes undergo apoptosis. Mice deficient for the PDCD1 gene bred on a BALB/c background developed dilated cardiomyopathy and died from congestive heart failure. These studies suggest that the PDCD1 gene product may also be important in T cell function and contribute to the prevention of autoimmune diseases.
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Synonyms
Programmed cell death protein 1, CD279, hPD-1, SLEB2, hPD-l, hSLE1, PD-1, PD1, PDCD1.
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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
PGWFLDSPDR PWNPPTFSPA LLVVTEGDNA TFTCSFSNTS ESFVLNWYRM SPSNQTDKLA AFPEDRSQPG QDCRFRVTQL PNGRDFHMSV VRARRNDSGT YLCGAISLAP KAQIKESLRA ELRVTERRAE VPTAHPSPSP RPAGQFQTLV LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK
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 :
Adiponectin Human, HEKDescription:
Adiponectin Human Recombinant, HEK
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-434Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Acrp30 Human Recombinant produced in HEK cells is a glycosylated polypeptide chain containing 234 amino acids (19-244a.a.) and having a molecular mass of 25.5kDa. Acrp30 is expressed with a FLAG tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 50mM phosphate Buffer, 75mM NaCl, pH 7.4.
Purity
Greater than 98% as determined by HPLC and SDS PAGE.
Biological Activity
In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.
sds-page
More Info
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Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
For long term, store lyophilized AdipoQ 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. The lyophilized protein remains stable for 24 months when stored at -20°C.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product not sterile! Please filter the product by an appropriate sterile filter before using it in cell culture.
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Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.
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Background
What is the molecular weight/Mw of adiponectin Protein?
Adiponectin Protein has a total Mw of 25.5kDa.
What is the source or expression system of adiponectin Protein?
HEK293.
What is the Purity of adiponectin Protein?
adiponectin Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of adiponectin Protein?
In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.
What is the amino acid sequence of adiponectin Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.
What applications can adiponectin Protein be used in?
adiponectin Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for adiponectin Protein?
The endotoxin level is minimal, adiponectin 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 :
CFLAR HumanDescription:
CASP8 and FADD-Like Apoptosis Regulator Human Recombinant
CASP8 and FADD-like apoptosis regulator, CASH, CLARP, Casper, I-FLICE, Inhibitor of FLICE, MRIT, c-FLIP, FLAME, FLAME-1, FADD-like antiapoptotic molecule 1, Caspase homolog, Caspase-eight-related protein, Caspase-like apoptosis regulatory protein, Cellular FLICE-like inhibitory protein, CASP8AP1, MACH-related inducer of toxicity, usurpin beta, CASPER.
Product # :
PRO-920Price :
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Description
CFLAR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 480 amino acids (1-480) and having a molecular mass of 55.3 kDa.The CFLAR is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CFLAR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
The precise role of CFLAR is not yet revealed but it seems it is vital in apoptosis regulation downstream of all identified death receptors.
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Synonyms
CASP8 and FADD-like apoptosis regulator, CASH, CLARP, Casper, I-FLICE, Inhibitor of FLICE, MRIT, c-FLIP, FLAME, FLAME-1, FADD-like antiapoptotic molecule 1, Caspase homolog, Caspase-eight-related protein, Caspase-like apoptosis regulatory protein, Cellular FLICE-like inhibitory protein, CASP8AP1, MACH-related inducer of toxicity, usurpin beta, CASPER.
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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
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN FRLHNGRSKE QRLKEQLGAQ QEPVKKSIQE SEAFLPQSIP EERYKMKSKP LGICLIIDCI GNETELLRDT FTSLGYEVQK FLHLSMHGIS QILGQFACMP EHRDYDSFVC VLVSRGGSQS VYGVDQTHSG LPLHHIRRMF MGDSCPYLAG KPKMFFIQNY VVSEGQLENS SLLEVDGPAM KNVEFKAQKR GLCTVHREAD FFWSLCTADM SLLEQSHSSP SLYLQCLSQK LRQERKRPLL DLHIELNGYM YDWNSRVSAK EKYYVWLQHT LRKKLILSYT.
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 :
SNRPD HumanDescription:
Small Nuclear Ribonucleoprotein Polypeptide D1, D2, D3 Human Recombinant
Product # :
PRO-997Price :
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Description
SNRPD Human Recombinant produced in SF9 insect cells, is a mixed protein complex containing the SNRPD1 (16 kDa), SNRPD2 (18 kDa) and SNRPD3 (18 kDa) proteins. Each protein (SNRPD1+ SNRPD2+ SNRPD3) is individually fused to a -6xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
SNRPD is supplied in 20mM HEPES buffer pH-7.5, 400mM NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative samples).
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coating concentration
0.4-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.
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Applications
Western blot with:
a) Anti-Sm positive patient sera.
b) Monoclonal anti-hexa-His-tag antibody.
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 :
COPZ1 HumanDescription:
Coatomer Protein Complex, Subunit Zeta 1 Human Recombinant
Coatomer protein complex subunit zeta 1, Zeta-1 COP, CGI-120, COPZ.
Product # :
PRO-221Price :
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Shipped with Ice Packs
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Description
COPZ1 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 197 amino acids (1-177a.a.) and having a molecular mass of 22.3kDa. The COPZ1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The COPZ1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
COPZ1 is a member of the adaptor complexes small subunit family. Coatomer is an oligomeric complex which contains as a minimum the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. The zeta subunit has a part in regulating the coat assembly and, therefore, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
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Synonyms
Coatomer protein complex subunit zeta 1, Zeta-1 COP, CGI-120, COPZ.
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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 MEALILEPSL YTVKAILILD NDGDRLFAKY YDDTYPSVKE QKAFEKNIFN KTHRTDSEIA LLEGLTVVYK SSIDLYFYVI GSSYENELML MAVLNCLFDS LSQMLRKNVE KRALLENMEG LFLAVDEIVD GGVILESDPQ QVVHRVALRG EDVPLTEQTV SQVLQSAKEQ IKWSLLR.
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 :
YWHAH HumanDescription:
Tyr-3/Trp-5 Monooxygenase Activation Protein ETA Human Recombinant
14-3-3 ETA, YWHAH, YWHA1, Protein AS1, Tyr-3/Trp-5 Monooxygenase Activation Protein ETA.
Product # :
PKA-087Price :
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Shipped with Ice Packs
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Description
YWHAH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 246 amino acids and having a molecular mass of 28.2kDa. The YWHAH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The YWHAH protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
YWHAH belongs to the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. 14-3-3 ETA is found in plants and mammals, and there is 99% identity to the mouse, rat and bovine orthologs. YWHAH gene contains a 7 base pair repeat sequence in its 5' UTR, and changes in the number of this repeat has been associated with early-onset schizophrenia.
14-3-3 eta is specific to the site of joint inflammation.
14-3-3 proteins are colocalized with Lewy bodies in Parkinson disease, though there is no specific staining for the 14-3-3 eta subunit.
There are 3 different isoforms types of 14-3-3: Beta, Gamma and ETA that are DAL-1/Protein 4.1B-binding proteins. -
Synonyms
14-3-3 ETA, YWHAH, YWHA1, Protein AS1, Tyr-3/Trp-5 Monooxygenase Activation Protein ETA.
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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
MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LSLLDKFLIK NCNDFQYESK VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEQMQPTHP IRLGLALNFS VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE EAGEGN.
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 :
Streptavidin ProteinDescription:
Streptavidin
Product # :
PRO-283Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Streptavidin is a protein produced by Streptomyces avidinii and isolated by purification from fermentation broth. The pure, homogeneous protein shows predominantly one single band in SDS PAGE. Streptavidin consists of 4 identical subunits, each bearing an active binding site for biotin. Streptavidin has a molecular weight of 55kDa.
Source
Bacterium Streptomyces avidinii.
Formulation
The Streptavidin was lyophilized from a 25mg/ml solution in 10 mM potassium phosphate buffer pH 6.5
More Info
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Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is wilyde used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Streptavidin although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. For longer storage in dissolved form add 1mM EDTA and/or 0.02 % NaN3 or pass the solution through a sterile filter.Please prevent freeze-thaw cycles.
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Solubility
Gives a clear solution at 10mg/ml in 4.0 mM potassium phosphate pH 6.5
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Specific Activity
The biological activity is 16.8 U/mg, 1 unit binds 1µg biotin.
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 :
ZNRD1 HumanDescription:
Zinc Ribbon Domain Containing 1 Human Recombinant
Zinc Ribbon Domain Containing 1, Zinc Ribbon Domain Containing, 1, HTEX-6, Rpa12, TEX6, ZR14, DNA-Directed RNA Polymerase I Subunit RPA12, hZR14, RNA Polymerase I Small Specific Subunit Rpa12, tctex-6, Transcription-Associated Zinc Ribbon Protein, RPA12, Zinc Ribbon Domain-Containing Protein 1.
Product # :
PRO-1747Price :
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Shipped with Ice Packs
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Description
ZNRD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids (1-126a.a) and having a molecular mass of 16.3kDa.ZNRD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ZNRD1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Zinc Ribbon Domain Containing 1 (ZNRD1) is a protein which shows similarity to the Saccharomyces cerevisiae Rpa12p subunit of RNA polymerase I. ZNRD1 contains two potential zinc-binding motifs and takes part in regulation of cell proliferation. ZNRD1 is involved in cancer and human immunodeficiency virus progression. Alternate splicing of this gene results in two transcript variants encoding the same protein. Additional splice variants have been found, but their full-length sequences have not been determined.
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Synonyms
Zinc Ribbon Domain Containing 1, Zinc Ribbon Domain Containing, 1, HTEX-6, Rpa12, TEX6, ZR14, DNA-Directed RNA Polymerase I Subunit RPA12, hZR14, RNA Polymerase I Small Specific Subunit Rpa12, tctex-6, Transcription-Associated Zinc Ribbon Protein, RPA12, Zinc Ribbon Domain-Containing Protein 1.
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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 MGSMSVMDLA NTCSSFQSDL DFCSDCGSVL PLPGAQDTVT CIRCGFNINV RDFEGKVVKT SVVFHQLGTA MPMSVEEGPE CQGPVVDRRC PRCGHEGMAY HTRQMRSADE GQTVFYTCTN CKFQEKEDS
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 :
STX17 HumanDescription:
Syntaxin-17 Human Recombinant
Syntaxin 17
Product # :
PRO-1712Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
STX17 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-229) and having a molecular mass of 28.6kDa.STX17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The STX17 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
STX17 is a member of to the syntaxin family and contains 1 t-SNARE coiled-coil homology domain. STX17 is involved in vesicle trafficking to lysosomes and takes part in procedures associated with cell division.
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Synonyms
Syntaxin 17
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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 MGSMSEDEEK VKLRRLEPAI QKFIKIVIPT DLERLRKHQI NIEKYQRCRI WDKLHEEHIN AGRTVQQLRS NIREIEKLCL KVRKDDLVLL KRMIDPVKEE ASAATAEFLQ LHLESVEELK KQFNDEETLL QPPLTRSMTV GGAFHTTEAE ASSQSLTQIY ALPEIPQDQN AAESWETLEA DLIELSQLVT DFSLLVNSQQ EKIDSIADHV NSAAVNVEEG TKNLGKAAKY KL
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 :
SERPINA5 Human, ActiveDescription:
Serpin Peptidase Inhibitor, Clade A Member 5 Human Recombinant, Active
Serpin Family A Member 5, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Acrosomal Serine Protease Inhibitor 3 4 Protein C Inhibitor, PLANH3, PAI-3, PROCI, PAI3, PCI, Plasminogen Activator Inhibitor III, Plasminogen Activator Inhibitor-3, Plasminogen Activator Inhibitor 3, Plasma Serine Protease Inhibitor, Serpin A5, PCI-B.
Product # :
PRO-2523Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SERPINA5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (20-406 a.a) and having a molecular mass of 45.9kDa.SERPINA5 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SERPINA5 protein solution (0.5mg/ml) contains 150mM NaCl, 10% glycerol & 20 mM MES buffer (pH6.0).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to inhibit Thrombin cleavage of substrate Boc-VPR-AMC. The IC50 for this effect is less or equal to 2 nM.
More Info
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Introduction
SERPINA5 up regulates TAFI activation by inhibiting the protein C activation. SERPINA5 is a significant regulator in the equilibrium between coagulation and fibrinolysis by differentially inhibiting the activation of TAFI and of Protein-C. SERPINA5 belongs to the serpin serine proteinase inhibitor family. SERPINA5 protein inhibits plasminogen activators as well as activated protein C.
SERPINA5 is secreted in plasma & liver. SERPINA5 is involved in cell inflammation, proliferation, apoptosis, tumour cell migration, invasion, and metastasis. Moreover, SERPINA5 controls the invasive potential of renal cell carcinoma by inhibiting urinary plasminogen activator secreted by the cells. SERPINA5 participtes in regulating key serine proteases which are involved in metastatic prostate disease. -
Synonyms
Serpin Family A Member 5, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Acrosomal Serine Protease Inhibitor 3 4 Protein C Inhibitor, PLANH3, PAI-3, PROCI, PAI3, PCI, Plasminogen Activator Inhibitor III, Plasminogen Activator Inhibitor-3, Plasminogen Activator Inhibitor 3, Plasma Serine Protease Inhibitor, Serpin A5, PCI-B.
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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 MHRHHPREMK KRVEDLHVGA TVAPSSRRDF TFDLYRALAS AAPSQNIFFS PVSISMSLAM LSLGAGSSTK MQILEGLGLN LQKSSEKELH RGFQQLLQEL NQPRDGFQLS LGNALFTDLV VDLQDTFVSA MKTLYLADTF PTNFRDSAGA MKQINDYVAK QTKGKIVDLL KNLDSNAVVI MVNYIFFKAK WETSFNHKGT QEQDFYVTSE TVVRVPMMSR EDQYHYLLDR NLSCRVVGVP YQGNATALFI LPSEGKMQQV ENGLSEKTLR KWLKMFKKRQ LELYLPKFSI EGSYQLEKVL PSLGISNVFT SHADLSGISN HSNIQVSEMV HKAVVEVDES GTRAAAATGT IFTFRSARLN SQRLVFNRPF LMFIVDNNIL FLGKVNRP.
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 :
CDC123 HumanDescription:
Cell Division Cycle 123 Human Recombinant
C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.
Product # :
PRO-1463Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDC123 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (1-336 a.a) and having a molecular mass of 41.5kDa.CDC123 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CDC123 protein solution (0. 5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CDC123 is a member of the CDC123 family. CDC123is required for S phase entry of the cell cycle. It is also broadly expressed in spleen,thymus, prostate, testis, ovary, small intestine, colon and leukocytes with the uppermost expression in testis.
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Synonyms
C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.
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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 MGSMKKEHVL HCQFSAWYPF FRGVTIKSVI LPLPQNVKDY LLDDGTLVVS GRDDPPTHSQ PDSDDEAEEI QWSDDENTAT LTAPEFPEFA TKVQEAINSL GGSVFPKLNW SAPRDAYWIA MNSSLKCKTL SDIFLLFKSS DFITRDFTQP FIHCTDDSPD PCIEYELVLR KWCELIPGAE FRCFVKENKL IGISQRDYTQ YYDHISKQKE EIRRCIQDFF KKHIQYKFLD EDFVFDIYRD SRGKVWLIDF NPFGEVTDSL LFTWEELISE NNLNGDFSEV DAQEQDSPAF RCTNSEVTVQ PSPYLSYRLP KDFVDLSTGE DAHKLIDFLK LKRNQQEDD
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 :
CBX3 HumanDescription:
Chromobox Homolog 3 Human Recombinant
Chromobox homolog 3 (Drosophila HP1 gamma), Heterochromatin protein 1 homolog gamma, Modifier 2 protein, HP1 gamma homolog, HECH, HP1Hs-gamma.
Product # :
PRO-1057Price :
Quantity :
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Shipped with Ice Packs
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Description
CBX3 Human Recombinant produced in E. coli is a single polypeptide chain containing 207 amino acids (1-183) and having a molecular mass of 23.4kDa.CBX3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CBX3 solution (1mg/ml) 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
CBX3 takes part in transcriptional silencing in heterochromatin-like complexes. CBX3 identifies and binds histone H3 tails methylated at 'Lys-9', thereby create an epigenetic repression. Additionally, CBX3 takes part in the formation of functional kinetochore by interacting with MIS12 complex proteins.
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Synonyms
Chromobox homolog 3 (Drosophila HP1 gamma), Heterochromatin protein 1 homolog gamma, Modifier 2 protein, HP1 gamma homolog, HECH, HP1Hs-gamma.
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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 MGSHMASNKT TLQKMGKKQN GKSKKVEEAE PEEFVVEKVL DRRVVNGKVE YFLKWKGFTD ADNTWEPEEN LDCPELIEAF LNSQKAGKEK DGTKRKSLSD SESDDSKSKK KRDAADKPRG FARGLDPERI IGATDSSGEL MFLMKWKDSD EADLVLAKEA NMKCPQIVIA FYEERLTWHS CPEDEAQ.
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 :
STX4 HumanDescription:
Syntaxin-4 Human Recombinant
Syntaxin 4, syntaxin 4A (placental), STX4A, Renal carcinoma antigen NY-REN-31, p35-2.
Product # :
PRO-1176Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
STX4 Human Recombinant produced in E. coli is a single polypeptide chain containing 300 amino acids (1-275) and having a molecular mass of 34.7 kDa.STX4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The STX4 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Syntaxin 4 (STX4) is a member of the syntaxin/epimorphin family of proteins. The Syntaxin family is cellular receptors for transport vesicles which participate in exocytosis in neutrophils. Syntaxin 4 is vital for normal regulation of glucose metabolism uptake in skeletal muscle and decline in STX4 protein levels lead to reduction of whole-body hormone-stimulated glucose metabolism. STX4 is expressed in neutrophils and neutrophil-differentiated HL-60 cells. The STX4 expression in neutrophils increases with differentiation.
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Synonyms
Syntaxin 4, syntaxin 4A (placental), STX4A, Renal carcinoma antigen NY-REN-31, p35-2.
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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 MGSHMMRDRT HELRQGDDSS DEEDKERVAL VVHPGTARLG SPDEEFFHKV RTIRQTIVKL GNKVQELEKQ QVTILATPLP EESMKQELQN LRDEIKQLGR EIRLQLKAIE PQKEEADENY NSVNTRMRKT QHGVLSQQFV ELINKCNSMQ SEYREKNVER IRRQLKITNA GMVSDEELEQ MLDSGQSEVF VSNILKDTQV TRQALNEISA RHSEIQQLER SIRELHDIFT FLATEVEMQG EMINRIEKNI LSSADYVERG QEHVKTALEN QKKARKKKVL
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 :
HSPA13 HumanDescription:
Heat shock 70kDa protein 13 Human Recombinant
Heat shock protein 70kDa family member 13, STCH, Stress 70 protein chaperone microsome-associated 60kD, Microsomal stress-70 protein ATPase core.
Product # :
HSP-041Price :
Quantity :
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Description
HSPA13 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 489 amino acids (23-471a.a.) and having a molecular mass of 54.3 kDa. HSPA13 is fused to a 40 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HSPA13 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
HSPA13 belongs to the heat shock protein 70 family and is related to microsomes. Members of this protein family take part in the processing of cytosolic and secretory proteins, in addition to the exclusion of denatured or incorrectly-folded proteins. HSPA13 is known to cooperate with PLIC-1 and PLIC-2, proteins which have a role in the signaling connection between the membrane receptors for thrombospondin and the cytoskeleton.
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Synonyms
Heat shock protein 70kDa family member 13, STCH, Stress 70 protein chaperone microsome-associated 60kD, Microsomal stress-70 protein ATPase core.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSELEM QQYLPLPTPK VIGIDLGTTY CSVGVFFPGT GKVKVIPDEN GHISIPSMVS FTDNDVYVGY ESVELADSNP QNTIYDAKRF IGKIFTAEEL EAEIGRYPFK VLNKNGMVEF SVTSNETITV SPEYVGSRLL LKLKEMAEAY LGMPVANAVI SVPAEFDLKQ RNSTIEAANL AGLKILRVIN EPTAAAMAYG LHKADVFHVL VIDLGGGTLD VSLLNKQGGM FLTRAMSGNN KLGGQDFNQR LLQYLYKQIY QTYGFVPSRK EEIHRLRQAV EMVKLNLTLH QSAQLSVLLT VEEQDRKEPH SSDTELPKDK LSSADDHRVN SGFGRGLSDK KSGESQVLFE TEISRKLFDT LNEDLFQKIL VPIQQVLKEG HLEKTEIDEV VLVGGSTRIP RIRQVIQEFF GKDPNTSVDP
DLAVVTGVAI QAGIDGGFWP LQVSALEIPN KHLQKTNFN.
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 :
OmpADescription:
Outer Membrane Protein-A Bacterial Recombinant
Outer Membrane Protein-A, OmpA.
Product # :
PRO-571Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The recombinant form was found to be undistinguishable from the wild type when examined by SDS-PAGE and gel filtration chromatography yielding a 50.5 kDa monomeric protein. The immunological similarity of the protein samples was demonstrated by employing polyclonal and monoclonal antibodies in ELISA and Western Blot techniques. All forms of A-protein were found to activate the secretion of tumour necrosis factor alpha from murine macrophage. For ref see Maurice et al. (1999) Protein Expression and Purification 16, 396-404.The OmpA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OmpA protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel filtration.
(b) Analysis by SDS-PAGE.Biological Activity
The interaction of bacterial and recombinant A-layer protein with murine macrophages was directed at determining the effect of A-protein on intracellular events that occur in primed macrophages. This was accomplished by measuring the cytotoxic product produced by peritoneal macrophages when exposed to A-protein coated latex beads. Thioglycolate elicited macrophages exhibited a low level of activation (18% cytotoxicity) that was significantly increased (48% cytotoxicity) in the presence of latex beads. Coating of the latex beads with each of the three A-protein products resulted in an increase of cytoxicity (mean +/- SEM) from 48% to 91%.More Info
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Introduction
The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.
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Synonyms
Outer Membrane Protein-A, OmpA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bacterial Outer Membrane Protein-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon C between 2-7 days and for future use reconstituted OmpA should be stored at 4 below -18°C. 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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Solubility
It is recommended to reconstitute the lyophilized OmpA in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
mdvvispndn tfvttslasv tkqpvldfst aqqnltlnfs evgdlknngf ivleiqgegq fndaeirqwl sngfwrrpft gllvnpndhg nfansgevnd vrkffkiisd gtqltivhti dsngkrlrla lasdveetin fadaevelkl nlanqafklt sgsqgtvalt agalwnasyt adpvatkplf klgklfqlsl tnagkatalv segflklnig danisatdfa itnvttnqti qrdkvnltlt gdvsafkkda ngnlvnkaga sigwkaaadg qsatavlgag nmaggvqnal aafgtlyvaa dntvpvpavn fnvkaeiqgd sqatynyfkd eladlfiltr dgmkfdtitt gttsanlihi rdvsnilpte ggkifvtite yadhaangrg egtvlvtrka lsvtlpsgga vtlkpadvaa dvgasitagr qarlvfevet nqgevavkks naegvdiqng trgtaplvdf tl.
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 :
Gly m 4.0101Description:
Stress-Induced Protein SAM22 Recombinant
Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.
Product # :
PRO-2278Price :
Quantity :
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Description
Recombinant Stress-Induced Protein SAM22 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 19,484 Dalton. Gly m 4.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Gly m 4.0101 is supplied in in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Stress-Induced Protein SAM22 (Gly m 4.0101) causes an allergic reaction in humans. Gly m 4 is the main soy allergen for patients allergic to birch pollen with soy allergy.
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Synonyms
Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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 :
RERG HumanDescription:
RAS-like, Estrogen-Regulated, Growth Inhibitor Human Recombinant
Ras-related and estrogen-regulated growth inhibitor, RERG, MGC15754.
Product # :
PRO-106Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RERG 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 219 amino acids (1-199 a.a.) and having a molecular mass of 24.7kDa (Molecular size on SDS-PAGE will appear higher). The RERG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RERG solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
RERG is a 199 amino acid protein which localizes in the cytoplasm and is a member of the Ras subfamily of small GTPases. RERG is expressed in the pancreas, liver, skin, lung, brain, kidney and heart tissue. RERG is a vital mediator of diverse cell signaling pathways, including those leading to cell proliferation, cytoskeletal organization and secretion.
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Synonyms
Ras-related and estrogen-regulated growth inhibitor, RERG, MGC15754.
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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 MAKSAEVKLA IFGRAGVGKS ALVVRFLTKR FIWEYDPTLE STYRHQATID DEVVSMEILD TAGQEDTIQR EGHMRWGEGF VLVYDITDRG SFEEVLPLKN ILDEIKKPKN VTLILVGNKA DLDHSRQVST EEGEKLATEL ACAFYECSAC TGEGNITEIF YELCREVRRR RMVQGKTRRR SSTTHVKQAI NKMLTKISS.
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 :
POMC HumanDescription:
Proopiomelanocortin Human Recombinant
Pro-opiomelanocortin, POMC, LPH, MSH, NPP, POC, ACTH, CLIP.
Product # :
PRO-236Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
POMC produced in E.Coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (27-267 a.a) and having a molecular mass of 28.9kDa (molecular weight on SDS-PAGE will appear higher).POMC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
POMC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 50% glycerol, 0.1mM PMSF, 0.1M Imidazole and 0.2M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Pro-opiomelanocortin preproprotein (POMC) is a polypeptide hormone precursor which experiences extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. POMC regulates the corticosteroid production in the adrenal cortex. Furthermore, POMC is cleaved into ten hormone chains named NPP, g-MSH, ACTH, a-MSH, CLIP, Lipotropin b, Lipotropin g, b-MSH,b endorphin and Met-enkephalin. POMC gene defects are the cause of POMC deficiency, which is characterized by red hair and adrenal insufficiency.
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Synonyms
Pro-opiomelanocortin, POMC, LPH, MSH, NPP, POC, ACTH, CLIP.
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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 MWCLESSQCQ DLTTESNLLE CIRACKPDLS AETPMFPGNG DEQPLTENPR KYVMGHFRWD RFGRRNSSSS GSSGAGQKRE DVSAGEDCGP LPEGGPEPRS DGAKPGPREG KRSYSMEHFR WGKPVGKKRR PVKVYPNGAE DESAEAFPLE FKRELTGQRL
REGDGPDGPA DDGAGAQADL EHSLLVAAEK KDEGPYRMEH FRWGSPPKDK RYGGFMTSEK SQTPLVTLFK NAIIKNAYKK GE.
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 :
Adiponectin Human, HMWDescription:
Adiponectin glycosylated Human Recombinant, HMW Rich
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-764Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
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Description
Adiponectin Human Recombinant HMW Rich produced in HEK cells is a single, glycosylated, polypeptide chain (19-244) containing a total of 226 amino acids, having a molecular mass of 24.6kDa (calculated). Human Acrp30 HMW Rich migrates on SDS-PAGE under non-reducing conditions at ~ 884 kDa.
Source
HEK293.
Formulation
Acrp30 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris, 50mM NaCl, pH 7.5 and 1mM CaCl2.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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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.
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Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Acrp30 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 24.6 kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
CXCL8 Human (1-77)Description:
Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8)
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Product # :
CHM-327Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- sds-page
Description
Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8904 Dalton. The IL-8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.
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 chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.sds-page
More Info
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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
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Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 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 Interleukin 8 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
AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.
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Background
What is the molecular weight/Mw of CXCL8 HUMAN (1-77) Protein?
CXCL8 HUMAN (1-77) Protein has a total Mw of 8.9kDa.
What is the source or expression system of CXCL8 HUMAN (1-77) Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN (1-77) Protein?
CXCL8 HUMAN (1-77) Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN (1-77) Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.
What is the amino acid sequence of CXCL8 HUMAN (1-77) Protein?
AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.
What applications can CXCL8 HUMAN (1-77) Protein be used in?
CXCL8 HUMAN (1-77) Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN (1-77) Protein?
The endotoxin level is minimal, CXCL8 HUMAN (1-77) 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 :
BLOC1S5 HumanDescription:
Biogenesis of Lysosomal Organelles Complex-1, Subunit 5 Human Recombinant
Biogenesis of lysosome-related organelles complex 1 subunit 5, BLOC-1 subunit 5, Protein Muted homolog, BLOC1S5, MUTED.
Product # :
PRO-1155Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
BLOC1S5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-187 a.a) and having a molecular mass of 24kDa.BLOC1S5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BLOC1S5 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 40% glycerol, 2mM DTT, 0.1mM PMSF and 1mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Muted homolog (MUTED) is a component of the BLOC-1 complex, a complex which is necessary for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. The BLOC-1 complex is needed to steer membrane protein cargos into vesicles assembled at cell bodies for release into neurites and nerve terminals. In addition, this complex, along with SNARE proteins, is suggested to be involved in neurite extension. MUTED also interacts with pallidin, dystrobrevin binding protein 1 and CNO/cappuccino. MUTED is ubiquitously expressed with higher levels in the brain, bone marrow, kidney, and liver and lower levels in the skeletal muscle.
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Synonyms
Biogenesis of lysosome-related organelles complex 1 subunit 5, BLOC-1 subunit 5, Protein Muted homolog, BLOC1S5, MUTED.
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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 MGSMSGGGTE TPVGCEAAPG GGSKKRDSLG TAGSAHLIIK DLGEIHSRLL DHRPVIQGET RYFVKEFEEK RGLREMRVLE NLKNMIHETN EHTLPKCRDT MRDSLSQVLQ RLQAANDSVC RLQQREQERK KIHSDHLVAS EKQHMLQWDN FMKEQPNKRA EVDEEHRKAM ERLKEQYAEM EKDLAKFSTF.
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.