Recombinant Human Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 (PLOD3)

Code CSB-YP018201HU
MSDS
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Source Yeast
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Code CSB-EP018201HU
MSDS
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Source E.coli
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Code CSB-EP018201HU-B
MSDS
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP018201HU
MSDS
Size Pls inquire
Source Baculovirus
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
PLOD3
Uniprot No.
Alternative Names
2-oxoglutarate 5-dioxygenase 3; bone protein I; BP-I; LH3; Lysine hydroxylase 3; Lysyl hydroxylase 3; Plod3; PLOD3_HUMAN; Procollagen lysine,2 oxoglutarate 5 dioxygenase 3 precursor; Procollagen-lysine
Species
Homo sapiens (Human)
Expression Region
25-738
Target Protein Sequence
SDRPRG RDPVNPEKLL VITVATAETE GYLRFLRSAE FFNYTVRTLG LGEEWRGGDV ARTVGGGQKV RWLKKEMEKY ADREDMIIMF VDSYDVILAG SPTELLKKFV QSGSRLLFSA ESFCWPEWGL AEQYPEVGTG KRFLNSGGFI GFATTIHQIV RQWKYKDDDD DQLFYTRLYL DPGLREKLSL NLDHKSRIFQ NLNGALDEVV LKFDRNRVRI RNVAYDTLPI VVHGNGPTKL QLNYLGNYVP NGWTPEGGCG FCNQDRRTLP GGQPPPRVFL AVFVEQPTPF LPRFLQRLLL LDYPPDRVTL FLHNNEVFHE PHIADSWPQL QDHFSAVKLV GPEEALSPGE ARDMAMDLCR QDPECEFYFS LDADAVLTNL QTLRILIEEN RKVIAPMLSR HGKLWSNFWG ALSPDEYYAR SEDYVELVQR KRVGVWNVPY ISQAYVIRGD TLRMELPQRD VFSGSDTDPD MAFCKSFRDK GIFLHLSNQH EFGRLLATSR YDTEHLHPDL WQIFDNPVDW KEQYIHENYS RALEGEGIVE QPCPDVYWFP LLSEQMCDEL VAEMEHYGQW SGGRHEDSRL AGGYENVPTV DIHMKQVGYE DQWLQLLRTY VGPMTESLFP GYHTKARAVM NFVVRYRPDE QPSLRPHHDS STFTLNVALN HKGLDYEGGG CRFLRYDCVI SSPRKGWALL HPGRLTHYHE GLPTTWGTRY IMVSFVDP
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen. Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine. Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues. Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues. Essential for normal biosynthesis and secretion of type IV collagens. Essential for normal formation of basement membranes.
Gene References into Functions
  1. VIPAR, with its partner proteins, regulate sorting of lysyl hydroxylase 3 (LH3, also known as PLOD3) into newly identified post-Golgi collagen IV carriers PMID: 27435297
  2. Proteomic analysis revealed that PLOD3, which is the gene encoding for collagen-modifying lysyl hydroxylase 3 (LH3), is regulated by miR-663a. PMID: 27233793
  3. The study shows that lysyl hydroxylase 3 localizes to epidermal basement membrane and is reduced in patients with recessive dystrophic epidermolysis bullosa. PMID: 26380979
  4. MMP-9 recruitment to the fibroblast cell surface by Lysyl Hydroxylase 3 (LH3) triggers TGF-beta activation and fibroblast differentiation PMID: 25825495
  5. LH3 molecules found in the cell medium are secreted through the Golgi complex, and the secretion is dependent on LH3 glycosyltransferase activity; LH3 found on the cell surface bypasses the Golgi complex PMID: 21465473
  6. Dimerization of human lysyl hydroxylase 3 is mediated by the amino acids 541-547 PMID: 20955792
  7. Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3. The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity PMID: 11956192
  8. Manipulation of the gene for LH3 can be used to selectively alter glycosylation and hydroxylation reactions, and provides new tool to clarify functions of unique hydroxylysine linked carbohydrates in collagens and other proteins. PMID: 12475640
  9. LH3 is present and active in the extracellular space PMID: 16447251
  10. The deficiency of LH3 glycosyltransferase activities, especially in the extracellular space, causes growth arrest. PMID: 18298658
  11. mutations of the lysyl hydroxylase 3 gene may cause a connective tissue disorder [case report] PMID: 18834968

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Involvement in disease
Lysyl hydroxylase 3 deficiency (LH3 deficiency)
Subcellular Location
Rough endoplasmic reticulum. Endoplasmic reticulum lumen. Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. Secreted. Secreted, extracellular space.
Tissue Specificity
Ubiquitous. Detected in heart, placenta and pancreas and at lower levels in lung, liver and skeletal muscle.
Database Links

HGNC: 9083

OMIM: 603066

KEGG: hsa:8985

STRING: 9606.ENSP00000223127

UniGene: Hs.153357

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