Difference between revisions of "Part:BBa K1898400"
(One intermediate revision by the same user not shown) | |||
Line 3: | Line 3: | ||
<partinfo>BBa_K1898400 short</partinfo> | <partinfo>BBa_K1898400 short</partinfo> | ||
− | This gene codes for | + | This gene codes for CRYAB, also known as crystallin alpha B, a crystallin protein exists in the lens and also other tissues and organs. |
===Usage and Biology=== | ===Usage and Biology=== | ||
Alpha crystallin is the most abundant protein in the lens. Out of the two types of alpha crystallin proteins, alpha B is less restricted to the lens and has a 1:3 ratio to alpha A [1]. It has been found that crystallin alpha B affects lens development and has chaperone activity to maintain normal protein interaction[2]. | Alpha crystallin is the most abundant protein in the lens. Out of the two types of alpha crystallin proteins, alpha B is less restricted to the lens and has a 1:3 ratio to alpha A [1]. It has been found that crystallin alpha B affects lens development and has chaperone activity to maintain normal protein interaction[2]. | ||
− | In our project, we made | + | In our project, we made CRYAB because we wanted to monitor crystallin protein's response to oxidative stress and to test our prevention and treatment for cataracts. |
[1]Genes and mapped phenotypes. (n.d.). from https://www.ncbi.nlm.nih.gov/gene/1410 | [1]Genes and mapped phenotypes. (n.d.). from https://www.ncbi.nlm.nih.gov/gene/1410 |
Latest revision as of 03:13, 20 October 2016
CRYAB, crystallin alpha B
This gene codes for CRYAB, also known as crystallin alpha B, a crystallin protein exists in the lens and also other tissues and organs.
Usage and Biology
Alpha crystallin is the most abundant protein in the lens. Out of the two types of alpha crystallin proteins, alpha B is less restricted to the lens and has a 1:3 ratio to alpha A [1]. It has been found that crystallin alpha B affects lens development and has chaperone activity to maintain normal protein interaction[2].
In our project, we made CRYAB because we wanted to monitor crystallin protein's response to oxidative stress and to test our prevention and treatment for cataracts.
[1]Genes and mapped phenotypes. (n.d.). from https://www.ncbi.nlm.nih.gov/gene/1410
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 26
Illegal BamHI site found at 368 - 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 453
Illegal SapI.rc site found at 313
Gel Picture
We designed primers to move CRYAB cDNA into iGEM BioBrick. PCR was set up and the gel picture is shown below. The expected band size is ~1kb, and the bands at the expected size are boxed in red.
Sequencing
We sent CRYAB out to sequencing after it's cloned into iGEM backbone. The sequencing file is annotated as follows:
- four restriction sites are highlighted in red
- CRYAB is highlighted in orange
This confirms that the sequence is correct (with no stop codon) and is moved into the BioBrick.